SitesBLAST
Comparing Echvi_4078 FitnessBrowser__Cola:Echvi_4078 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)
49% identity, 92% coverage: 33:467/475 of query aligns to 35:469/485 of 2f2aA
- active site: K79 (= K76), S154 (= S151), S155 (= S152), S173 (≠ T170), T175 (= T172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (= Q178)
- binding glutamine: G130 (= G127), S154 (= S151), D174 (= D171), T175 (= T172), G176 (= G173), S178 (= S175), F206 (≠ Y203), Y309 (= Y306), Y310 (= Y307), R358 (= R355), D425 (= D422)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
49% identity, 92% coverage: 33:467/475 of query aligns to 35:469/485 of 2dqnA
- active site: K79 (= K76), S154 (= S151), S155 (= S152), S173 (≠ T170), T175 (= T172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (= Q178)
- binding asparagine: M129 (= M126), G130 (= G127), T175 (= T172), G176 (= G173), S178 (= S175), Y309 (= Y306), Y310 (= Y307), R358 (= R355), D425 (= D422)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 96% coverage: 6:463/475 of query aligns to 6:458/478 of 3h0mA
- active site: K72 (= K76), S147 (= S151), S148 (= S152), S166 (≠ T170), T168 (= T172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (= Q178)
- binding glutamine: M122 (= M126), G123 (= G127), D167 (= D171), T168 (= T172), G169 (= G173), G170 (= G174), S171 (= S175), F199 (≠ Y203), Y302 (= Y306), R351 (= R355), D418 (= D422)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 96% coverage: 6:463/475 of query aligns to 6:458/478 of 3h0lA
- active site: K72 (= K76), S147 (= S151), S148 (= S152), S166 (≠ T170), T168 (= T172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (= Q178)
- binding asparagine: G123 (= G127), S147 (= S151), G169 (= G173), G170 (= G174), S171 (= S175), Y302 (= Y306), R351 (= R355), D418 (= D422)
3kfuE Crystal structure of the transamidosome (see paper)
45% identity, 94% coverage: 9:455/475 of query aligns to 4:438/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 86% coverage: 48:454/475 of query aligns to 10:433/450 of 4n0iA
- active site: K38 (= K76), S116 (= S151), S117 (= S152), T135 (= T170), T137 (= T172), G138 (= G173), G139 (= G174), S140 (= S175), L143 (≠ Q178)
- binding glutamine: G89 (= G127), T137 (= T172), G138 (= G173), S140 (= S175), Y168 (= Y203), Y271 (= Y306), Y272 (= Y307), R320 (= R355), D404 (= D422)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 88% coverage: 50:467/475 of query aligns to 178:584/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G125), T258 (≠ S128), S281 (= S151), G302 (≠ T172), G303 (= G173), S305 (= S175), S472 (≠ M339), I532 (≠ D413), M539 (≠ L420)
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, 88% coverage: 50:467/475 of query aligns to 178:584/607 of Q7XJJ7
- K205 (= K76) mutation to A: Loss of activity.
- SS 281:282 (= SS 151:152) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 172:175) binding
- S305 (= S175) mutation to A: Loss of activity.
- R307 (= R177) mutation to A: Loss of activity.
- S360 (≠ Q230) mutation to A: No effect.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 97% coverage: 14:473/475 of query aligns to 37:489/507 of Q84DC4
- K100 (= K76) mutation to A: Abolishes activity on mandelamide.
- S180 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S152) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G173) 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 (= S175) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q178) 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 (≠ V302) 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 (≠ D369) 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.
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.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
28% identity, 97% coverage: 9:467/475 of query aligns to 10:472/487 of 1m21A
- active site: K81 (= K76), S160 (= S151), S161 (= S152), T179 (= T170), T181 (= T172), D182 (≠ G173), G183 (= G174), S184 (= S175), C187 (≠ Q178)
- binding : A129 (≠ G125), N130 (≠ M126), F131 (≠ G127), C158 (≠ G149), G159 (= G150), S160 (= S151), S184 (= S175), C187 (≠ Q178), I212 (≠ Y203), R318 (≠ Y307), L321 (≠ T310), L365 (≠ M357), F426 (≠ Y419)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 89% coverage: 52:474/475 of query aligns to 71:500/508 of 3a1iA
- active site: K95 (= K76), S170 (= S151), S171 (= S152), G189 (≠ T170), Q191 (≠ T172), G192 (= G173), G193 (= G174), A194 (≠ S175), I197 (≠ Q178)
- binding benzamide: F145 (≠ M126), S146 (≠ G127), G147 (≠ S128), Q191 (≠ T172), G192 (= G173), G193 (= G174), A194 (≠ S175), W327 (≠ Y306)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
27% identity, 95% coverage: 9:461/475 of query aligns to 5:438/457 of 6c6gA
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 88% coverage: 47:463/475 of query aligns to 62:453/605 of Q936X2
- K91 (= K76) mutation to A: Loss of activity.
- S165 (= S151) mutation to A: Loss of activity.
- S189 (= S175) mutation to A: Loss of activity.
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)
46% identity, 24% coverage: 101:214/475 of query aligns to 63:176/425 of Q9FR37
- S113 (= S151) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S152) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D171) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S175) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ T183) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 36 active site, Charge relay system; K→A: Loss of catalytic activity.; K→R: Reduces catalytic activity 10-fold.
- 214 S→T: Slightly reduces catalytic activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
26% identity, 98% coverage: 6:470/475 of query aligns to 3:406/412 of 1o9oA
- active site: K62 (= K76), A131 (≠ S151), S132 (= S152), T150 (= T170), T152 (= T172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ Q178)
- binding 3-amino-3-oxopropanoic acid: G130 (= G150), T152 (= T172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ Q178), P359 (= P415)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 90% coverage: 46:472/475 of query aligns to 44:439/461 of 4gysB
- active site: K72 (= K76), S146 (= S151), S147 (= S152), T165 (= T170), T167 (= T172), A168 (≠ G173), G169 (= G174), S170 (= S175), V173 (≠ Q178)
- binding malonate ion: A120 (≠ G125), G122 (= G127), S146 (= S151), T167 (= T172), A168 (≠ G173), S170 (= S175), S193 (≠ F198), G194 (= G199), V195 (≠ L200), R200 (≠ S205), Y297 (= Y328), R305 (≠ N335)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
26% identity, 98% coverage: 6:470/475 of query aligns to 3:406/412 of 1ocmA
- active site: K62 (= K76), S131 (= S151), S132 (= S152), T152 (= T172), G153 (= G173), G154 (= G174), S155 (= S175)
- binding pyrophosphate 2-: R113 (≠ N130), S131 (= S151), Q151 (≠ D171), T152 (= T172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ Q178), P359 (= P415)
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
45% identity, 23% coverage: 108:216/475 of query aligns to 103:211/593 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)
31% identity, 39% coverage: 65:249/475 of query aligns to 58:248/482 of 3a2qA
- active site: K69 (= K76), S147 (= S151), S148 (= S152), N166 (≠ T170), A168 (≠ T172), A169 (≠ G173), G170 (= G174), A171 (≠ S175), I174 (≠ Q178)
- binding 6-aminohexanoic acid: G121 (= G125), G121 (= G125), N122 (≠ M126), S147 (= S151), A168 (≠ T172), A168 (≠ T172), A169 (≠ G173), A171 (≠ S175)
Sites not aligning to the query:
1mt5A Crystal structure of fatty acid amide hydrolase (see paper)
27% identity, 49% coverage: 58:291/475 of query aligns to 88:324/537 of 1mt5A
- active site: K106 (= K76), S181 (= S151), S182 (= S152), T200 (= T170), I202 (≠ T172), G203 (= G173), G204 (= G174), S205 (= S175), F208 (≠ Q178)
- binding methyl arachidonyl fluorophosphonate: M155 (≠ G125), L156 (≠ M126), S157 (≠ G127), S181 (= S151), D201 (= D171), I202 (≠ T172), G203 (= G173), S205 (= S175)
Sites not aligning to the query:
Query Sequence
>Echvi_4078 FitnessBrowser__Cola:Echvi_4078
MEKFHSFDEIKRSLENKETDCKAIVHYYLKNIQTKAHLNAFVEVYEQSALEQAEKVDQKI
KAGTAGKLAGMVIGIKDVLCYADHEVNASSKILEGFQSQFTATAVQKLIDEDAIIIGRLN
CDEFGMGSSNENTVHGKVLNALDEGRVPGGSSGGSAVAVQANLCTTSLGTDTGGSVRQPA
AFTGLVGIKPTYSRVSRFGLIAYASSFDTIGVFSTNVKDNALVLEVIAGQDDNDSTVSRK
AVPHYSEQLQLDRPVKVAYLKETIESEALQPAIKEHTLDILDKLKEEGHQVEEVDFPLLE
YVLPTYYILTTAEASSNLSRFDGVKYGYRTPNAHNLESMYKLTRSEGFGEEVKRRIMLGT
FVLSASYYDAYFTKAQKVRRLIKEFTEDLLNKFDYIVLPTTPSTAFKFGEHSDDPVAMYL
EDLYTVQASVSGVPAISIPNGKDENGLPIGLQVITNSFKEAELYAFADYLMKIKK
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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