SitesBLAST
Comparing 3607637 FitnessBrowser__Dino:3607637 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)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 90% coverage: 32:370/376 of query aligns to 63:462/478 of 3h0mA
- active site: K72 (= K41), S147 (= S116), S148 (= S117), S166 (= S135), T168 (= T137), G169 (≠ L138), G170 (= G139), S171 (= S140), Q174 (≠ I143)
- binding glutamine: M122 (≠ L91), G123 (= G92), D167 (= D136), T168 (= T137), G169 (≠ L138), G170 (= G139), S171 (= S140), F199 (≠ L168), Y302 (≠ A257), R351 (= R303), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 90% coverage: 32:370/376 of query aligns to 63:462/478 of 3h0lA
- active site: K72 (= K41), S147 (= S116), S148 (= S117), S166 (= S135), T168 (= T137), G169 (≠ L138), G170 (= G139), S171 (= S140), Q174 (≠ I143)
- binding asparagine: G123 (= G92), S147 (= S116), G169 (≠ L138), G170 (= G139), S171 (= S140), Y302 (≠ A257), R351 (= R303), D418 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 89% coverage: 32:367/376 of query aligns to 56:447/468 of 3kfuE
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
28% identity, 90% coverage: 33:370/376 of query aligns to 197:584/607 of Q7XJJ7
- K205 (= K41) mutation to A: Loss of activity.
- SS 281:282 (= SS 116:117) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TLGS 137:140) binding
- S305 (= S140) mutation to A: Loss of activity.
- R307 (= R142) mutation to A: Loss of activity.
- S360 (≠ E195) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 90% coverage: 33:370/376 of query aligns to 197:584/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A90), T258 (≠ A93), S281 (= S116), G302 (≠ T137), G303 (≠ L138), S305 (= S140), S472 (≠ P283), I532 (vs. gap), M539 (≠ A331)
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)
48% identity, 42% coverage: 32:189/376 of query aligns to 65:223/457 of 6c6gA
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
40% identity, 50% coverage: 31:218/376 of query aligns to 69:252/485 of 2f2aA
- active site: K79 (= K41), S154 (= S116), S155 (= S117), S173 (= S135), T175 (= T137), G176 (≠ L138), G177 (= G139), S178 (= S140), Q181 (≠ I143)
- binding glutamine: G130 (= G92), S154 (= S116), D174 (= D136), T175 (= T137), G176 (≠ L138), S178 (= S140), F206 (≠ L168)
Sites not aligning to the query:
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
40% identity, 50% coverage: 31:218/376 of query aligns to 69:252/485 of 2dqnA
- active site: K79 (= K41), S154 (= S116), S155 (= S117), S173 (= S135), T175 (= T137), G176 (≠ L138), G177 (= G139), S178 (= S140), Q181 (≠ I143)
- binding asparagine: M129 (≠ L91), G130 (= G92), T175 (= T137), G176 (≠ L138), S178 (= S140)
Sites not aligning to the query:
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)
38% identity, 43% coverage: 33:192/376 of query aligns to 28:189/425 of Q9FR37
- K36 (= K41) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S116) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S117) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D136) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S140) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C148) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
39% identity, 41% coverage: 32:185/376 of query aligns to 91:249/507 of Q84DC4
- K100 (= K41) mutation to A: Abolishes activity on mandelamide.
- S180 (≠ G118) mutation to A: Significantly decreases activity on mandelamide.
- S181 (≠ G119) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ L138) 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 (= S140) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I143) 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.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
40% identity, 43% coverage: 32:193/376 of query aligns to 72:237/487 of 1m21A
- active site: K81 (= K41), S160 (= S116), S161 (= S117), T179 (≠ S135), T181 (= T137), D182 (≠ L138), G183 (= G139), S184 (= S140), C187 (≠ I143)
- binding : A129 (= A90), N130 (≠ L91), F131 (≠ G92), C158 (≠ G114), G159 (= G115), S160 (= S116), S184 (= S140), C187 (≠ I143), I212 (≠ L168)
Sites not aligning to the query:
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
37% identity, 46% coverage: 22:193/376 of query aligns to 76:247/508 of 3a1iA
- active site: K95 (= K41), S170 (= S116), S171 (= S117), G189 (≠ S135), Q191 (≠ T137), G192 (≠ L138), G193 (= G139), A194 (≠ S140), I197 (= I143)
- binding benzamide: F145 (≠ L91), S146 (≠ G92), G147 (≠ A93), Q191 (≠ T137), G192 (≠ L138), G193 (= G139), A194 (≠ S140)
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
33% identity, 92% coverage: 30:376/376 of query aligns to 58:470/482 of 3a2qA
- active site: K69 (= K41), S147 (= S116), S148 (= S117), N166 (≠ S135), A168 (≠ T137), A169 (≠ L138), G170 (= G139), A171 (≠ S140), I174 (= I143)
- binding 6-aminohexanoic acid: G121 (≠ A90), G121 (≠ A90), N122 (≠ L91), S147 (= S116), A168 (≠ T137), A168 (≠ T137), A169 (≠ L138), A171 (≠ S140), C313 (≠ A262)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
39% identity, 43% coverage: 33:192/376 of query aligns to 30:192/450 of 4n0iA
- active site: K38 (= K41), S116 (= S116), S117 (= S117), T135 (≠ S135), T137 (= T137), G138 (≠ L138), G139 (= G139), S140 (= S140), L143 (≠ I143)
- binding glutamine: G89 (= G92), T137 (= T137), G138 (≠ L138), S140 (= S140), Y168 (≠ L168)
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
41% identity, 35% coverage: 31:161/376 of query aligns to 67:197/457 of 5h6sC
- active site: K77 (= K41), S152 (= S116), S153 (= S117), L173 (≠ T137), G174 (≠ L138), G175 (= G139), S176 (= S140)
- binding 4-oxidanylbenzohydrazide: C126 (vs. gap), R128 (≠ A93), W129 (≠ A94), S152 (= S116), L173 (≠ T137), G174 (≠ L138), S176 (= S140)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 85% coverage: 32:350/376 of query aligns to 82:431/605 of Q936X2
- K91 (= K41) mutation to A: Loss of activity.
- S165 (= S116) mutation to A: Loss of activity.
- S189 (= S140) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
41% identity, 41% coverage: 30:185/376 of query aligns to 51:200/412 of 1o9oA
- active site: K62 (= K41), A131 (≠ S116), S132 (= S117), T150 (≠ S135), T152 (= T137), G153 (≠ L138), G154 (= G139), S155 (= S140), R158 (≠ I143)
- binding 3-amino-3-oxopropanoic acid: G130 (= G115), T152 (= T137), G153 (≠ L138), G154 (= G139), S155 (= S140), R158 (≠ I143)
Sites not aligning to the query:
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
31% identity, 50% coverage: 73:261/376 of query aligns to 103:286/593 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.
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
42% identity, 41% coverage: 30:185/376 of query aligns to 51:200/412 of 1ocmA
- active site: K62 (= K41), S131 (= S116), S132 (= S117), T152 (= T137), G153 (≠ L138), G154 (= G139), S155 (= S140)
- binding pyrophosphate 2-: R113 (≠ G92), S131 (= S116), Q151 (≠ D136), T152 (= T137), G153 (≠ L138), G154 (= G139), S155 (= S140), R158 (≠ I143)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
42% identity, 42% coverage: 26:184/376 of query aligns to 58:214/461 of 4gysB
- active site: K72 (= K41), S146 (= S116), S147 (= S117), T165 (≠ S135), T167 (= T137), A168 (≠ L138), G169 (= G139), S170 (= S140), V173 (≠ I143)
- binding malonate ion: A120 (= A90), G122 (= G92), S146 (= S116), T167 (= T137), A168 (≠ L138), S170 (= S140), S193 (≠ G163), G194 (= G164), V195 (= V165), R200 (≠ P170)
Sites not aligning to the query:
Query Sequence
>3607637 FitnessBrowser__Dino:3607637
MTDAARLRALDDRFAFLEDPSTQVIPGSGTGPLAGLRIGVKSNIAVAGQAWTAGIAGRGE
VLAEADAEVIARLRAAGADLLPGLTMDEAALGAATETSGLRATQNPFAPGHSVGGSSGGA
AAAVACGAVPVALGSDTLGSVRIPAAYCGVLGFKPGAGVLPLGGVVPLDPALDTLGLLAR
RVADLRAVYAVLAPEAVAETAQVVQLAPQADVACAPEVQTALARAARLLDASGPDRLEGW
EAEALRMAAFTRVCAAAATTLADQPIASVAVRSAMAYGARLTPDGLARAEALCDRVAAAL
RARLPPGTVALTPTTPTPAFARGTPPPADQASFTVLANLAGLPAISVPMGPASVQLMAGP
GQEGTLLALADRLSAA
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