SitesBLAST
Comparing BWI76_RS13990 FitnessBrowser__Koxy:BWI76_RS13990 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)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
47% identity, 88% coverage: 69:597/598 of query aligns to 81:603/605 of Q936X2
- K91 (= K79) mutation to A: Loss of activity.
- S165 (= S153) mutation to A: Loss of activity.
- S189 (= S177) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
49% identity, 71% coverage: 44:467/598 of query aligns to 37:455/461 of 4gysB
- active site: K72 (= K79), S146 (= S153), S147 (= S154), T165 (= T172), T167 (= T174), A168 (= A175), G169 (= G176), S170 (= S177), V173 (= V180)
- binding malonate ion: A120 (= A127), G122 (= G129), S146 (= S153), T167 (= T174), A168 (= A175), S170 (= S177), S193 (≠ A200), G194 (= G201), V195 (= V202), R200 (= R207), Y297 (= Y308), R305 (= R316)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 75% coverage: 10:456/598 of query aligns to 7:477/478 of 3h0mA
- active site: K72 (= K79), S147 (≠ G152), S148 (= S153), S166 (≠ T172), T168 (= T174), G169 (≠ A175), G170 (= G176), S171 (= S177), Q174 (≠ V180)
- binding glutamine: M122 (≠ T128), G123 (= G129), D167 (= D173), T168 (= T174), G169 (≠ A175), G170 (= G176), S171 (= S177), F199 (≠ A205), Y302 (≠ E294), R351 (≠ V338), D418 (≠ N404)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 75% coverage: 10:456/598 of query aligns to 7:477/478 of 3h0lA
- active site: K72 (= K79), S147 (≠ G152), S148 (= S153), S166 (≠ T172), T168 (= T174), G169 (≠ A175), G170 (= G176), S171 (= S177), Q174 (≠ V180)
- binding asparagine: G123 (= G129), S147 (≠ G152), G169 (≠ A175), G170 (= G176), S171 (= S177), Y302 (≠ E294), R351 (≠ V338), D418 (≠ N404)
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 72% coverage: 19:451/598 of query aligns to 11:456/468 of 3kfuE
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 65% coverage: 70:455/598 of query aligns to 72:485/487 of 1m21A
- active site: K81 (= K79), S160 (= S153), S161 (= S154), T179 (= T172), T181 (= T174), D182 (≠ A175), G183 (= G176), S184 (= S177), C187 (≠ V180)
- binding : A129 (= A127), N130 (≠ T128), F131 (vs. gap), C158 (≠ G151), G159 (= G152), S160 (= S153), S184 (= S177), C187 (≠ V180), I212 (≠ A205), R318 (vs. gap), L321 (= L306), L365 (≠ V338), F426 (≠ L388)
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)
36% identity, 28% coverage: 71:236/598 of query aligns to 28:199/425 of Q9FR37
- K36 (= K79) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S153) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S154) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D173) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S177) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N185) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 64% coverage: 71:450/598 of query aligns to 197:589/607 of Q7XJJ7
- K205 (= K79) mutation to A: Loss of activity.
- SS 281:282 (= SS 153:154) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 174:177) binding
- S305 (= S177) mutation to A: Loss of activity.
- R307 (= R179) mutation to A: Loss of activity.
- S360 (≠ Y232) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 64% coverage: 71:450/598 of query aligns to 197:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A127), T258 (≠ L130), S281 (= S153), G302 (≠ T174), G303 (≠ A175), S305 (= S177), S472 (≠ V331), I532 (= I393), M539 (≠ G400)
Sites not aligning to the query:
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
25% identity, 73% coverage: 18:454/598 of query aligns to 16:478/485 of 2f2aA
- active site: K79 (= K79), S154 (= S153), S155 (= S154), S173 (≠ T172), T175 (= T174), G176 (≠ A175), G177 (= G176), S178 (= S177), Q181 (≠ V180)
- binding glutamine: G130 (= G129), S154 (= S153), D174 (= D173), T175 (= T174), G176 (≠ A175), S178 (= S177), F206 (≠ A205), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ V338), D425 (≠ G400)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
25% identity, 73% coverage: 18:454/598 of query aligns to 16:478/485 of 2dqnA
- active site: K79 (= K79), S154 (= S153), S155 (= S154), S173 (≠ T172), T175 (= T174), G176 (≠ A175), G177 (= G176), S178 (= S177), Q181 (≠ V180)
- binding asparagine: M129 (≠ T128), G130 (= G129), T175 (= T174), G176 (≠ A175), S178 (= S177), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ V338), D425 (≠ G400)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
27% identity, 66% coverage: 70:466/598 of query aligns to 73:559/564 of 6te4A
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
26% identity, 68% coverage: 47:450/598 of query aligns to 60:498/508 of 3a1iA
- active site: K95 (= K79), S170 (= S153), S171 (= S154), G189 (≠ T172), Q191 (≠ T174), G192 (≠ A175), G193 (= G176), A194 (≠ S177), I197 (≠ V180)
- binding benzamide: F145 (≠ T128), S146 (≠ G129), G147 (≠ L130), Q191 (≠ T174), G192 (≠ A175), G193 (= G176), A194 (≠ S177), W327 (≠ Q283)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
38% identity, 24% coverage: 69:211/598 of query aligns to 90:238/507 of Q84DC4
- K100 (= K79) mutation to A: Abolishes activity on mandelamide.
- S180 (= S153) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S154) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A175) 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 (= S177) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V180) 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.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- 316 S→N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- 382 Q→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.
- 437 I→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.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
33% identity, 28% coverage: 71:239/598 of query aligns to 30:202/450 of 4n0iA
- active site: K38 (= K79), S116 (vs. gap), S117 (vs. gap), T135 (= T172), T137 (= T174), G138 (≠ A175), G139 (= G176), S140 (= S177), L143 (≠ V180)
- binding glutamine: G89 (= G129), T137 (= T174), G138 (≠ A175), S140 (= S177), Y168 (≠ A205)
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)
34% identity, 32% coverage: 70:262/598 of query aligns to 65:259/457 of 6c6gA
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
36% identity, 24% coverage: 76:220/598 of query aligns to 66:213/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
25% identity, 73% coverage: 18:451/598 of query aligns to 15:470/482 of 3a2qA
- active site: K69 (= K79), S147 (= S153), S148 (= S154), N166 (≠ T172), A168 (≠ T174), A169 (= A175), G170 (= G176), A171 (≠ S177), I174 (≠ V180)
- binding 6-aminohexanoic acid: G121 (≠ A127), G121 (≠ A127), N122 (≠ T128), S147 (= S153), A168 (≠ T174), A168 (≠ T174), A169 (= A175), A171 (≠ S177), C313 (≠ L301)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 32% coverage: 4:197/598 of query aligns to 1:196/457 of 5h6sC
- active site: K77 (= K79), S152 (= S153), S153 (= S154), L173 (≠ T174), G174 (≠ A175), G175 (= G176), S176 (= S177)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A127), R128 (≠ G129), W129 (≠ L130), S152 (= S153), L173 (≠ T174), G174 (≠ A175), S176 (= S177)
Sites not aligning to the query:
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
28% identity, 33% coverage: 8:202/598 of query aligns to 77:266/579 of Q9TUI8
- S217 (= S153) mutation to A: Loss of activity.
- S218 (= S154) mutation to A: Lowers activity by at least 98%.
- D237 (= D173) mutation D->E,N: Loss of activity.
- S241 (= S177) mutation to A: Loss of activity.
- C249 (≠ N185) mutation to A: Loss of activity.
Query Sequence
>BWI76_RS13990 FitnessBrowser__Koxy:BWI76_RS13990
MMQQTFDLRLATLAADYRNGKTTPRRLLAEVRQRAQALNPEFRLFIHILSEEEQEPLLAA
LEGLSPTELPLYGVPFAIKDNIDLAEIITTAACPAFAYRAEQSATIVAQLIALGAVPVGK
TNLDQFATGLNGTRSPYGACRNGYLADYPSGGSSAGSALAVALGVASFSLGTDTAGSGRV
PAGLNNLVGLKATKGLISTAGVVPACRTLDCVTFFSATADEASQLLALVAQYDPLDAWSR
HNPQWNSRQAFGRPAAGFRFGVPRELNFLGCSASERLFTQARQRLTALGGVAVEIEFAPF
LAAARLLYDGPWVAERYAVVGPLMARQPEAVLPVIREVLAKAPDTDATATFKAIYQLQQY
KARCDAILETLDCVLTPTYPRPVTLDELQAEPIARNADLGYYTNFMNLLDYAAVSVPCGF
MPDGLPSGVTLFGRAFTDQYLLSLADAFQRAERLPLAGGTRLETPPPERAAGHDRMALVV
CGAHLAGLPLNDQLLARGGQLLQETRSAPHYRLYALADGKRPAMVRDESGGAAIAVEVWE
LPSAEVGSLLAAIPAPLGLGKVELADGRRLTGFICEAEGLGEATEITAYGGWRAWLAR
Or try a new SitesBLAST search
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