SitesBLAST
Comparing GFF3953 FitnessBrowser__Marino:GFF3953 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)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
38% identity, 97% coverage: 11:495/499 of query aligns to 3:480/482 of 3a2qA
- active site: K69 (= K77), S147 (= S153), S148 (= S154), N166 (= N172), A168 (≠ G174), A169 (≠ G175), G170 (= G176), A171 (≠ S177), I174 (= I180)
- binding 6-aminohexanoic acid: G121 (= G127), G121 (= G127), N122 (≠ L128), S147 (= S153), A168 (≠ G174), A168 (≠ G174), A169 (≠ G175), A171 (≠ S177), C313 (≠ V319)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 96% coverage: 16:495/499 of query aligns to 8:475/478 of 3h0mA
- active site: K72 (= K77), S147 (= S153), S148 (= S154), S166 (≠ N172), T168 (≠ G174), G169 (= G175), G170 (= G176), S171 (= S177), Q174 (≠ I180)
- binding glutamine: M122 (≠ L128), G123 (≠ K129), D167 (= D173), T168 (≠ G174), G169 (= G175), G170 (= G176), S171 (= S177), F199 (≠ T208), Y302 (≠ F302), R351 (≠ I344), D418 (≠ S430)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 96% coverage: 16:495/499 of query aligns to 8:475/478 of 3h0lA
- active site: K72 (= K77), S147 (= S153), S148 (= S154), S166 (≠ N172), T168 (≠ G174), G169 (= G175), G170 (= G176), S171 (= S177), Q174 (≠ I180)
- binding asparagine: G123 (≠ K129), S147 (= S153), G169 (= G175), G170 (= G176), S171 (= S177), Y302 (≠ F302), R351 (≠ I344), D418 (≠ S430)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 96% coverage: 15:493/499 of query aligns to 8:483/490 of 4yjiA
- active site: K79 (= K77), S158 (= S153), S159 (= S154), G179 (= G174), G180 (= G175), G181 (= G176), A182 (≠ S177)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L79), G132 (= G127), S158 (= S153), G179 (= G174), G180 (= G175), A182 (≠ S177)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 87% coverage: 56:487/499 of query aligns to 181:592/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G127), T258 (≠ A130), S281 (= S153), G302 (= G174), G303 (= G175), S305 (= S177), S472 (≠ I344), I532 (≠ Q425), M539 (≠ A432)
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)
28% identity, 87% coverage: 56:487/499 of query aligns to 181:592/607 of Q7XJJ7
- K205 (= K77) mutation to A: Loss of activity.
- SS 281:282 (= SS 153:154) mutation to AA: Loss of activity.
- GGGS 302:305 (= GGGS 174:177) binding
- S305 (= S177) mutation to A: Loss of activity.
- R307 (= R179) mutation to A: Loss of activity.
- S360 (≠ P233) mutation to A: No effect.
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 93% coverage: 22:486/499 of query aligns to 9:457/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 86% coverage: 66:495/499 of query aligns to 68:485/485 of 2f2aA
- active site: K79 (= K77), S154 (= S153), S155 (= S154), S173 (≠ N172), T175 (≠ G174), G176 (= G175), G177 (= G176), S178 (= S177), Q181 (≠ I180)
- binding glutamine: G130 (≠ K129), S154 (= S153), D174 (= D173), T175 (≠ G174), G176 (= G175), S178 (= S177), F206 (≠ T208), Y309 (≠ F302), Y310 (≠ D303), R358 (≠ I344), D425 (≠ S430)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 86% coverage: 66:495/499 of query aligns to 68:485/485 of 2dqnA
- active site: K79 (= K77), S154 (= S153), S155 (= S154), S173 (≠ N172), T175 (≠ G174), G176 (= G175), G177 (= G176), S178 (= S177), Q181 (≠ I180)
- binding asparagine: M129 (≠ L128), G130 (≠ K129), T175 (≠ G174), G176 (= G175), S178 (= S177), Y309 (≠ F302), Y310 (≠ D303), R358 (≠ I344), D425 (≠ S430)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 85% coverage: 62:484/499 of query aligns to 80:498/508 of 3a1iA
- active site: K95 (= K77), S170 (= S153), S171 (= S154), G189 (≠ N172), Q191 (≠ G174), G192 (= G175), G193 (= G176), A194 (≠ S177), I197 (= I180)
- binding benzamide: F145 (≠ L128), S146 (≠ K129), G147 (≠ A130), Q191 (≠ G174), G192 (= G175), G193 (= G176), A194 (≠ S177), W327 (vs. gap)
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)
31% identity, 56% coverage: 18:295/499 of query aligns to 82:360/579 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.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
35% identity, 35% coverage: 71:244/499 of query aligns to 75:250/487 of 1m21A
- active site: K81 (= K77), S160 (= S153), S161 (= S154), T179 (≠ N172), T181 (≠ G174), D182 (≠ G175), G183 (= G176), S184 (= S177), C187 (≠ I180)
- binding : A129 (≠ G127), N130 (vs. gap), F131 (≠ L128), C158 (≠ G151), G159 (= G152), S160 (= S153), S184 (= S177), C187 (≠ I180), I212 (≠ E205)
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)
27% identity, 93% coverage: 22:484/499 of query aligns to 10:449/457 of 6c6gA
3qkvA Crystal structure of fatty acid amide hydrolase with small molecule compound (see paper)
30% identity, 55% coverage: 22:293/499 of query aligns to 58:330/549 of 3qkvA
- active site: K114 (= K77), S189 (= S153), S190 (= S154), T208 (≠ N172), I210 (≠ G174), G211 (= G175), G212 (= G176), S213 (= S177), F216 (≠ I180)
- binding (6-bromo-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidin]-1'-yl)methanol: L164 (= L128), S165 (≠ K129), I210 (≠ G174), G211 (= G175), S213 (= S177)
Sites not aligning to the query:
3qk5A Crystal structure of fatty acid amide hydrolase with small molecule inhibitor (see paper)
30% identity, 55% coverage: 22:293/499 of query aligns to 58:330/549 of 3qk5A
- active site: K114 (= K77), S189 (= S153), S190 (= S154), T208 (≠ N172), I210 (≠ G174), G211 (= G175), G212 (= G176), S213 (= S177), F216 (≠ I180)
- binding (3-{(3R)-1-[4-(1-benzothiophen-2-yl)pyrimidin-2-yl]piperidin-3-yl}-2-methyl-1H-pyrrolo[2,3-b]pyridin-1-yl)acetonitrile: L164 (= L128), S165 (≠ K129), I210 (≠ G174), G211 (= G175), G212 (= G176), S213 (= S177), F216 (≠ I180)
Sites not aligning to the query:
3qj9A Crystal structure of fatty acid amide hydrolase with small molecule inhibitor (see paper)
30% identity, 55% coverage: 22:293/499 of query aligns to 58:330/549 of 3qj9A
- active site: K114 (= K77), S189 (= S153), S190 (= S154), T208 (≠ N172), I210 (≠ G174), G211 (= G175), G212 (= G176), S213 (= S177), F216 (≠ I180)
- binding 1-{(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl}-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one: L164 (= L128), S165 (≠ K129), F166 (≠ A130), I210 (≠ G174)
Sites not aligning to the query:
1mt5A Crystal structure of fatty acid amide hydrolase (see paper)
30% identity, 55% coverage: 22:293/499 of query aligns to 50:322/537 of 1mt5A
- active site: K106 (= K77), S181 (= S153), S182 (= S154), T200 (≠ N172), I202 (≠ G174), G203 (= G175), G204 (= G176), S205 (= S177), F208 (≠ I180)
- binding methyl arachidonyl fluorophosphonate: M155 (≠ G127), L156 (= L128), S157 (≠ K129), S181 (= S153), D201 (= D173), I202 (≠ G174), G203 (= G175), S205 (= S177)
Sites not aligning to the query:
P97612 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 Rattus norvegicus (Rat) (see paper)
30% identity, 55% coverage: 22:293/499 of query aligns to 86:358/579 of P97612
- K142 (= K77) mutation to A: Lowers activity 40000-fold. Lowers activity 70000-fold; when associated with A-217.
- S217 (= S153) mutation to A: Lowers activity 3000-fold. Lowers activity 70000-fold; when associated with A-142.
4do3A Structure of faah with a non-steroidal anti-inflammatory drug (see paper)
30% identity, 55% coverage: 22:293/499 of query aligns to 54:326/543 of 4do3A
- active site: K110 (= K77), S185 (= S153), S186 (= S154), T204 (≠ N172), I206 (≠ G174), G207 (= G175), G208 (= G176), S209 (= S177), F212 (≠ I180)
- binding (2S)-2-(6-chloro-9H-carbazol-2-yl)propanoic acid: L160 (= L128)
- binding cyclohexane aminocarboxylic acid: L160 (= L128), I206 (≠ G174), G207 (= G175), S209 (= S177)
Sites not aligning to the query:
4hbpA Crystal structure of faah in complex with inhibitor (see paper)
30% identity, 55% coverage: 22:293/499 of query aligns to 50:316/531 of 4hbpA
- active site: K100 (= K77), S175 (= S153), S176 (= S154), T194 (≠ N172), I196 (≠ G174), G197 (= G175), G198 (= G176), S199 (= S177), F202 (≠ I180)
- binding 4-(3-phenyl-1,2,4-thiadiazol-5-yl)-N-(pyridin-3-yl)piperazine-1-carboxamide: S151 (≠ K129), F152 (≠ A130), I196 (≠ G174), G197 (= G175), S199 (= S177)
Sites not aligning to the query:
Query Sequence
>GFF3953 FitnessBrowser__Marino:GFF3953
MEPAMKQSEYLRYDATALADLIRRGEVTSGEVCEAAVERATRVNGKLNAICYPQFSEAPA
QPFPEQGVFAGVPLLLKDLAQEQADHPCTYGSRGMTKNIAPRDSEFVRRARNGGLVFLGR
TATPEFGLKAVTESELWGPTRNPWNTQLTPGGSSGGSGAAAAAGIVPMAGANDGGGSIRI
PAAYNGLFGLKPSRGRISSGPFMGEAWTGASTDHVVSRTVRDSAAMLDVLSGPAPGDPFV
IPQPPAPYAELVQRSPGSLKIGVFTSSPYNTEVAPECVAAVEETARVLESLGHRVEYAAP
EFDGMALARCYLGLYFGEVSALMAKAKEQFGAADSDFELDTRLIGMLGNTMPLSDYVRRR
QQWNEFARALGVFFGRYDLYLSPTTGQLPAAIGELETPAHLKFAARLMLKLNAGKLVHRT
GQVDQMALESLARTPFTQLANLTGTPAMSVPMHWTAEGLPVGVQLGGPHGAEATLLQLAG
QLEEANPWFGNYERLEDAF
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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