SitesBLAST
Comparing HSERO_RS02850 FitnessBrowser__HerbieS:HSERO_RS02850 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
37% identity, 74% coverage: 48:526/651 of query aligns to 2:486/487 of 1m21A
- active site: K81 (= K127), S160 (= S202), S161 (= S203), T179 (≠ S221), T181 (= T223), D182 (≠ C224), G183 (= G225), S184 (= S226), C187 (≠ I229)
- binding : A129 (= A176), N130 (≠ A177), F131 (vs. gap), C158 (≠ G200), G159 (= G201), S160 (= S202), S184 (= S226), C187 (≠ I229), I212 (≠ L254), R318 (vs. gap), L321 (≠ I365), L365 (≠ S410), F426 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
36% identity, 68% coverage: 74:517/651 of query aligns to 22:455/468 of 3kfuE
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 65% coverage: 98:517/651 of query aligns to 176:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A176), T258 (≠ V179), S281 (= S202), G302 (≠ T223), G303 (≠ C224), S305 (= S226), S472 (= S410), I532 (≠ C470), M539 (vs. gap)
Sites not aligning to the query:
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 65% coverage: 98:517/651 of query aligns to 176:589/607 of Q7XJJ7
- K205 (= K127) mutation to A: Loss of activity.
- SS 281:282 (= SS 202:203) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TCGS 223:226) binding
- S305 (= S226) mutation to A: Loss of activity.
- R307 (= R228) mutation to A: Loss of activity.
- S360 (= S281) mutation to A: No effect.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 72% coverage: 49:519/651 of query aligns to 2:469/478 of 3h0mA
- active site: K72 (= K127), S147 (= S202), S148 (= S203), S166 (= S221), T168 (= T223), G169 (≠ C224), G170 (= G225), S171 (= S226), Q174 (≠ I229)
- binding glutamine: M122 (≠ A177), G123 (= G178), D167 (= D222), T168 (= T223), G169 (≠ C224), G170 (= G225), S171 (= S226), F199 (≠ L254), Y302 (≠ S362), R351 (≠ E421), D418 (≠ A474)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 72% coverage: 49:519/651 of query aligns to 2:469/478 of 3h0lA
- active site: K72 (= K127), S147 (= S202), S148 (= S203), S166 (= S221), T168 (= T223), G169 (≠ C224), G170 (= G225), S171 (= S226), Q174 (≠ I229)
- binding asparagine: G123 (= G178), S147 (= S202), G169 (≠ C224), G170 (= G225), S171 (= S226), Y302 (≠ S362), R351 (≠ E421), D418 (≠ A474)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
31% identity, 74% coverage: 49:531/651 of query aligns to 2:564/564 of 6te4A
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 76% coverage: 38:535/651 of query aligns to 13:504/507 of Q84DC4
- T31 (= T55) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K127) mutation to A: Abolishes activity on mandelamide.
- S180 (= S202) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S203) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ C224) mutation to A: Increase in KM values for aromatic substrates, but not aliphatic substrates. Active against lactamide but not against mandelamide; when associated with H-207 and E-382.; mutation to V: Increase in KM values for aromatic substrates, but not aliphatic substrates.
- S204 (= S226) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I229) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with E-382. Active against lactamide but not against mandelamide; when associated with A-202 and E-382. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with S-316 and N-437.
- S316 (≠ L359) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- Q382 (≠ E421) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with H-207. Active against lactamide but not against mandelamide; when associated with A-202 and H-207.
- I437 (vs. gap) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with I-31. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-316.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 67% coverage: 81:518/651 of query aligns to 32:475/485 of 2f2aA
- active site: K79 (= K127), S154 (= S202), S155 (= S203), S173 (= S221), T175 (= T223), G176 (≠ C224), G177 (= G225), S178 (= S226), Q181 (≠ I229)
- binding glutamine: G130 (= G178), S154 (= S202), D174 (= D222), T175 (= T223), G176 (≠ C224), S178 (= S226), F206 (≠ L254), Y309 (≠ G361), Y310 (≠ S362), R358 (≠ K424), D425 (≠ C470)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 67% coverage: 81:518/651 of query aligns to 32:475/485 of 2dqnA
- active site: K79 (= K127), S154 (= S202), S155 (= S203), S173 (= S221), T175 (= T223), G176 (≠ C224), G177 (= G225), S178 (= S226), Q181 (≠ I229)
- binding asparagine: M129 (≠ A177), G130 (= G178), T175 (= T223), G176 (≠ C224), S178 (= S226), Y309 (≠ G361), Y310 (≠ S362), R358 (≠ K424), D425 (≠ C470)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
33% identity, 46% coverage: 55:355/651 of query aligns to 8:299/457 of 5h6sC
- active site: K77 (= K127), S152 (= S202), S153 (= S203), L173 (≠ T223), G174 (≠ C224), G175 (= G225), S176 (= S226)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A176), R128 (≠ G178), W129 (≠ V179), S152 (= S202), L173 (≠ T223), G174 (≠ C224), S176 (= S226)
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
40% identity, 40% coverage: 63:320/651 of query aligns to 12:264/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 64% coverage: 117:530/651 of query aligns to 85:507/508 of 3a1iA
- active site: K95 (= K127), S170 (= S202), S171 (= S203), G189 (≠ S221), Q191 (≠ T223), G192 (≠ C224), G193 (= G225), A194 (≠ S226), I197 (= I229)
- binding benzamide: F145 (≠ A177), S146 (≠ G178), G147 (≠ V179), Q191 (≠ T223), G192 (≠ C224), G193 (= G225), A194 (≠ S226), W327 (≠ S362)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
34% identity, 41% coverage: 77:344/651 of query aligns to 44:301/605 of Q936X2
- K91 (= K127) mutation to A: Loss of activity.
- S165 (= S202) mutation to A: Loss of activity.
- S189 (= S226) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 62% coverage: 118:521/651 of query aligns to 63:443/461 of 4gysB
- active site: K72 (= K127), S146 (= S202), S147 (= S203), T165 (≠ S221), T167 (= T223), A168 (≠ C224), G169 (= G225), S170 (= S226), V173 (≠ I229)
- binding malonate ion: A120 (= A176), G122 (= G178), S146 (= S202), T167 (= T223), A168 (≠ C224), S170 (= S226), S193 (= S249), G194 (= G250), V195 (= V251), R200 (≠ S256), Y297 (≠ A393), R305 (≠ L400)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
28% identity, 72% coverage: 44:512/651 of query aligns to 3:464/482 of 3a2qA
- active site: K69 (= K127), S147 (= S202), S148 (= S203), N166 (≠ S221), A168 (≠ T223), A169 (≠ C224), G170 (= G225), A171 (≠ S226), I174 (= I229)
- binding 6-aminohexanoic acid: G121 (≠ A176), G121 (≠ A176), N122 (≠ A177), S147 (= S202), A168 (≠ T223), A168 (≠ T223), A169 (≠ C224), A171 (≠ S226), C313 (≠ L377)
Q9FR37 Amidase 1; AtAMI1; Translocon at the outer membrane of chloroplasts 64-I; AtTOC64-I; EC 3.5.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 60% coverage: 119:511/651 of query aligns to 28:417/425 of Q9FR37
- K36 (= K127) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S202) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S203) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D222) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S226) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ Q234) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ G302) mutation to T: Slightly reduces catalytic activity.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
34% identity, 27% coverage: 115:289/651 of query aligns to 26:203/450 of 4n0iA
- active site: K38 (= K127), S116 (= S202), S117 (= S203), T135 (≠ S221), T137 (= T223), G138 (≠ C224), G139 (= G225), S140 (= S226), L143 (≠ I229)
- binding glutamine: G89 (= G178), T137 (= T223), G138 (≠ C224), S140 (= S226), Y168 (≠ L254)
Sites not aligning to the query:
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
26% identity, 69% coverage: 79:527/651 of query aligns to 30:479/490 of 4yjiA
- active site: K79 (= K127), S158 (= S202), S159 (= S203), G179 (≠ T223), G180 (≠ C224), G181 (= G225), A182 (≠ S226)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N129), G132 (≠ A176), S158 (= S202), G179 (≠ T223), G180 (≠ C224), A182 (≠ S226)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
32% identity, 37% coverage: 117:354/651 of query aligns to 52:264/412 of 1o9oA
- active site: K62 (= K127), A131 (≠ S202), S132 (= S203), T150 (≠ S221), T152 (= T223), G153 (≠ C224), G154 (= G225), S155 (= S226), R158 (≠ I229)
- binding 3-amino-3-oxopropanoic acid: G130 (= G201), T152 (= T223), G153 (≠ C224), G154 (= G225), S155 (= S226), R158 (≠ I229)
Sites not aligning to the query:
Query Sequence
>HSERO_RS02850 FitnessBrowser__HerbieS:HSERO_RS02850
MKYHSNNTSSFARASSVVFTAMLLGAMTQTSFAQGKETASQRRLAQDPVFEASITHLQSA
QDAGRATSRSLVLAYLARIRAYDQQGPSLNAIVTLNPKALEEADQLDRERRQSGPRGPLH
GIPILVKDNYDTVDMPTTGGTLALATLQAQADAFQVKRLREAGAVILGKTTMHELAAGVT
TVSSLTGFTRNPYDPRRAPGGSSGGTGAAVAASFAAAGMGSDTCGSIRIPAAHQNLFGLR
TTRGLASRSGVMPLSSTQDVAAPLARSVEDLAIMLDATVGSDPQDSSTVDANGHIPKSYR
DGLRADSLQGARIGVLRALFGAAPEDAEVSAAINKALQQLKDQGAIVTDVTIPELDGLLS
GSSIIPYEFKYDLGAYLQSHPGAPVGSLGEILARGMEHELLEAGLRLRNSVDLQNPKDKE
ELEKVMLKRSALKSLMTDVMQKNHLDTLVYPTIQRKAALIGEPQGGAMNCQLSATTGLPA
LALPVGFTEDGLPVSLELLAPEFAEPALLGLAYGWEQKIGPRRSPYSTPALVAGKAPGLR
RIKPIVLDQPGDASVRVELAYDPVTARLDYQASARKVAASDVISLALQRGEADKPGPVVA
NLLRQHQKSVKASIVLQGKDREALLAGKLYVDFYTRSAPLGAGRQPLVLAD
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory