SitesBLAST
Comparing AO356_09120 FitnessBrowser__pseudo5_N2C3_1:AO356_09120 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
31% identity, 94% coverage: 21:448/453 of query aligns to 23:474/485 of 2f2aA
- active site: K79 (= K77), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (= T176), G176 (≠ A177), G177 (= G178), S178 (= S179), Q181 (≠ V182)
- binding glutamine: G130 (≠ S129), S154 (= S155), D174 (= D175), T175 (= T176), G176 (≠ A177), S178 (= S179), F206 (≠ L207), Y309 (vs. gap), Y310 (vs. gap), R358 (= R333), D425 (≠ L398)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
31% identity, 94% coverage: 21:448/453 of query aligns to 23:474/485 of 2dqnA
- active site: K79 (= K77), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (= T176), G176 (≠ A177), G177 (= G178), S178 (= S179), Q181 (≠ V182)
- binding asparagine: M129 (≠ Y128), G130 (≠ S129), T175 (= T176), G176 (≠ A177), S178 (= S179), Y309 (vs. gap), Y310 (vs. gap), R358 (= R333), D425 (≠ L398)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
41% identity, 51% coverage: 7:236/453 of query aligns to 1:231/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 91% coverage: 39:450/453 of query aligns to 62:490/507 of Q84DC4
- K100 (= K77) mutation to A: Abolishes activity on mandelamide.
- S180 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A177) 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 (= S179) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V182) 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 (≠ R287) 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 (≠ A342) 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 (≠ L398) 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.
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.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 96% coverage: 13:449/453 of query aligns to 135:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A127), T258 (≠ G130), S281 (= S155), G302 (≠ T176), G303 (≠ A177), S305 (= S179), S472 (≠ R333), I532 (≠ L389), M539 (≠ L398)
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)
26% identity, 96% coverage: 13:449/453 of query aligns to 135:590/607 of Q7XJJ7
- K205 (= K77) mutation to A: Loss of activity.
- SS 281:282 (= SS 155:156) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 176:179) binding
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
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)
31% identity, 84% coverage: 71:450/453 of query aligns to 30:425/425 of Q9FR37
- K36 (= K77) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S155) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S156) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D175) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S179) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N187) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ A255) mutation to T: Slightly reduces catalytic activity.
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 95% coverage: 17:447/453 of query aligns to 10:454/468 of 3kfuE
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
41% identity, 37% coverage: 69:235/453 of query aligns to 73:240/487 of 1m21A
- active site: K81 (= K77), S160 (= S155), S161 (= S156), T179 (= T174), T181 (= T176), D182 (≠ A177), G183 (= G178), S184 (= S179), C187 (≠ V182)
- binding : A129 (= A127), N130 (≠ Y128), F131 (vs. gap), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ V182), I212 (≠ L207)
Sites not aligning to the query:
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 77% coverage: 103:449/453 of query aligns to 120:499/508 of 3a1iA
- active site: S170 (= S155), S171 (= S156), G189 (≠ T174), Q191 (≠ T176), G192 (≠ A177), G193 (= G178), A194 (≠ S179), I197 (≠ V182)
- binding benzamide: F145 (≠ Y128), S146 (= S129), G147 (= G130), Q191 (≠ T176), G192 (≠ A177), G193 (= G178), A194 (≠ S179), W327 (≠ S295)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
33% identity, 92% coverage: 25:443/453 of query aligns to 20:434/461 of 4gysB
- active site: K72 (= K77), S146 (= S155), S147 (= S156), T165 (= T174), T167 (= T176), A168 (= A177), G169 (= G178), S170 (= S179), V173 (= V182)
- binding malonate ion: A120 (= A127), G122 (≠ S129), S146 (= S155), T167 (= T176), A168 (= A177), S170 (= S179), S193 (≠ D202), G194 (= G203), V195 (= V204), R200 (≠ H209), Y297 (≠ R300), R305 (≠ E309)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
32% identity, 87% coverage: 59:452/453 of query aligns to 74:467/605 of Q936X2
- K91 (= K77) mutation to A: Loss of activity.
- S165 (= S155) mutation to A: Loss of activity.
- S189 (= S179) mutation to A: Loss of activity.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 97% coverage: 12:452/453 of query aligns to 10:471/478 of 3h0mA
- active site: K72 (= K77), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (= T176), G169 (≠ A177), G170 (= G178), S171 (= S179), Q174 (≠ V182)
- binding glutamine: M122 (≠ Y128), G123 (≠ S129), D167 (= D175), T168 (= T176), G169 (≠ A177), G170 (= G178), S171 (= S179), F199 (≠ L207), Y302 (vs. gap), R351 (= R333), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 97% coverage: 12:452/453 of query aligns to 10:471/478 of 3h0lA
- active site: K72 (= K77), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (= T176), G169 (≠ A177), G170 (= G178), S171 (= S179), Q174 (≠ V182)
- binding asparagine: G123 (≠ S129), S147 (= S155), G169 (≠ A177), G170 (= G178), S171 (= S179), Y302 (vs. gap), R351 (= R333), D418 (vs. gap)
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
41% identity, 36% coverage: 74:238/453 of query aligns to 66:235/593 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.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
25% identity, 84% coverage: 65:446/453 of query aligns to 26:449/450 of 4n0iA
- active site: K38 (= K77), S116 (= S155), S117 (= S156), T135 (= T174), T137 (= T176), G138 (≠ A177), G139 (= G178), S140 (= S179), L143 (≠ V182)
- binding glutamine: G89 (≠ S129), T137 (= T176), G138 (≠ A177), S140 (= S179), Y168 (≠ L207), Y271 (≠ H302), Y272 (≠ G303), R320 (= R333), D404 (≠ L398)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 93% coverage: 25:447/453 of query aligns to 23:444/457 of 5h6sC
- active site: K77 (= K77), S152 (= S155), S153 (= S156), L173 (≠ T176), G174 (≠ A177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A127), R128 (≠ S129), W129 (≠ G130), S152 (= S155), L173 (≠ T176), G174 (≠ A177), S176 (= S179), W306 (= W304), F338 (≠ E335)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
32% identity, 53% coverage: 2:243/453 of query aligns to 1:248/490 of 4yjiA
- active site: K79 (= K77), S158 (= S155), S159 (= S156), G179 (≠ T176), G180 (≠ A177), G181 (= G178), A182 (≠ S179)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L79), G132 (≠ A127), S158 (= S155), G179 (≠ T176), G180 (≠ A177), A182 (≠ S179)
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)
32% identity, 47% coverage: 12:222/453 of query aligns to 82:288/579 of Q9TUI8
- S217 (= S155) mutation to A: Loss of activity.
- S218 (= S156) mutation to A: Lowers activity by at least 98%.
- D237 (= D175) mutation D->E,N: Loss of activity.
- S241 (= S179) mutation to A: Loss of activity.
- C249 (≠ N187) mutation to A: Loss of activity.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
32% identity, 50% coverage: 12:236/453 of query aligns to 10:241/564 of 6te4A
Sites not aligning to the query:
Query Sequence
>AO356_09120 FitnessBrowser__pseudo5_N2C3_1:AO356_09120
MSPFSSLDAIALAEAFASGRTDPVQVLEQALEQAARAEHVFVSLTEARARREAQASAARW
RAGQPLSGFDGVPMAWKDLFDVAGSVTTAAAAVRRNAPPALLDAASVSLLSRAGMVCLGK
TNLSEFAYSGLGLNPHFGTPVNPFSDAQPRIPGGSSSGSAVAVAAGIVPIAMGTDTAGSI
RVPAAFNALVGFRASSRRHNRDGVFPLAHSIDSIGPLTRSVRDAWMIDELLQGRDPRQAP
PVRSLAGQRFWVEQAVLEDARVEAAVRANVLAGVQALRTAGALVEIRPLPAFQASLALIR
DHGWLGAAEAFALHEALLDSADAERLDPRVRRRLEAARPMTASQVLKLYDARSTLQRQLV
EELDGAVLITPTVAHVAPPLAPLEADDELFARTNLATLSLTMPGSLLDMPGVNLPSGRDS
QGLPTGLLLSVPQGEDARLLRVARSVEAMLANS
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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