SitesBLAST
Comparing GFF1044 FitnessBrowser__Marino:GFF1044 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)
34% identity, 91% coverage: 19:472/498 of query aligns to 6:473/482 of 3a2qA
- active site: K69 (= K90), S147 (= S165), S148 (= S166), N166 (= N184), A168 (≠ G186), A169 (≠ G187), G170 (= G188), A171 (≠ S189), I174 (= I192)
- binding 6-aminohexanoic acid: G121 (= G139), G121 (= G139), N122 (≠ F140), S147 (= S165), A168 (≠ G186), A168 (≠ G186), A169 (≠ G187), A171 (≠ S189), C313 (≠ Y319)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 90% coverage: 21:469/498 of query aligns to 8:468/478 of 3h0mA
- active site: K72 (= K90), S147 (= S165), S148 (= S166), S166 (≠ N184), T168 (≠ G186), G169 (= G187), G170 (= G188), S171 (= S189), Q174 (≠ I192)
- binding glutamine: M122 (≠ F140), G123 (≠ N141), D167 (= D185), T168 (≠ G186), G169 (= G187), G170 (= G188), S171 (= S189), F199 (≠ L218), Y302 (≠ D315), R351 (≠ M354), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 90% coverage: 21:469/498 of query aligns to 8:468/478 of 3h0lA
- active site: K72 (= K90), S147 (= S165), S148 (= S166), S166 (≠ N184), T168 (≠ G186), G169 (= G187), G170 (= G188), S171 (= S189), Q174 (≠ I192)
- binding asparagine: G123 (≠ N141), S147 (= S165), G169 (= G187), G170 (= G188), S171 (= S189), Y302 (≠ D315), R351 (≠ M354), D418 (vs. gap)
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, 80% coverage: 74:471/498 of query aligns to 189:592/607 of Q7XJJ7
- K205 (= K90) mutation to A: Loss of activity.
- SS 281:282 (= SS 165:166) mutation to AA: Loss of activity.
- GGGS 302:305 (= GGGS 186:189) binding
- S305 (= S189) mutation to A: Loss of activity.
- R307 (= R191) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 80% coverage: 74:471/498 of query aligns to 189:592/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G139), T258 (≠ A142), S281 (= S165), G302 (= G186), G303 (= G187), S305 (= S189), S472 (vs. gap), I532 (≠ F411), M539 (≠ V418)
Sites not aligning to the query:
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
25% identity, 89% coverage: 27:470/498 of query aligns to 15:476/485 of 2f2aA
- active site: K79 (= K90), S154 (= S165), S155 (= S166), S173 (≠ N184), T175 (≠ G186), G176 (= G187), G177 (= G188), S178 (= S189), Q181 (≠ I192)
- binding glutamine: G130 (≠ N141), S154 (= S165), D174 (= D185), T175 (≠ G186), G176 (= G187), S178 (= S189), F206 (≠ L218), Y309 (= Y319), Y310 (≠ W320), R358 (≠ M354), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
25% identity, 89% coverage: 27:470/498 of query aligns to 15:476/485 of 2dqnA
- active site: K79 (= K90), S154 (= S165), S155 (= S166), S173 (≠ N184), T175 (≠ G186), G176 (= G187), G177 (= G188), S178 (= S189), Q181 (≠ I192)
- binding asparagine: M129 (≠ F140), G130 (≠ N141), T175 (≠ G186), G176 (= G187), S178 (= S189), Y309 (= Y319), Y310 (≠ W320), R358 (≠ M354), D425 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 89% coverage: 26:467/498 of query aligns to 8:454/468 of 3kfuE
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
35% identity, 44% coverage: 20:236/498 of query aligns to 8:230/490 of 4yjiA
- active site: K79 (= K90), S158 (= S165), S159 (= S166), G179 (= G186), G180 (= G187), G181 (= G188), A182 (≠ S189)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (vs. gap), G132 (= G139), S158 (= S165), G179 (= G186), G180 (= G187), A182 (≠ S189)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 76% coverage: 89:467/498 of query aligns to 94:497/508 of 3a1iA
- active site: K95 (= K90), S170 (= S165), S171 (= S166), G189 (≠ N184), Q191 (≠ G186), G192 (= G187), G193 (= G188), A194 (≠ S189), I197 (= I192)
- binding benzamide: F145 (= F140), S146 (≠ N141), G147 (≠ A142), Q191 (≠ G186), G192 (= G187), G193 (= G188), A194 (≠ S189), W327 (vs. gap)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 58% coverage: 19:307/498 of query aligns to 7:308/487 of 1m21A
- active site: K81 (= K90), S160 (= S165), S161 (= S166), T179 (≠ N184), T181 (≠ G186), D182 (≠ G187), G183 (= G188), S184 (= S189), C187 (≠ I192)
- binding : A129 (≠ G139), N130 (vs. gap), F131 (= F140), C158 (≠ G163), G159 (≠ A164), S160 (= S165), S184 (= S189), C187 (≠ I192), I212 (≠ L218)
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 91% coverage: 20:471/498 of query aligns to 7:448/457 of 5h6sC
- active site: K77 (= K90), S152 (= S165), S153 (= S166), L173 (≠ G186), G174 (= G187), G175 (= G188), S176 (= S189)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G139), R128 (≠ N141), W129 (≠ A142), S152 (= S165), L173 (≠ G186), G174 (= G187), S176 (= S189), W306 (= W320), F338 (≠ W360)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 90% coverage: 19:468/498 of query aligns to 32:488/507 of Q84DC4
- K100 (= K90) mutation to A: Abolishes activity on mandelamide.
- S180 (= S165) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S166) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G187) 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 (= S189) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I192) 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 (≠ D315) 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 (vs. gap) 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 (≠ V418) 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.
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)
26% identity, 83% coverage: 23:436/498 of query aligns to 82:509/579 of Q9TUI8
- S217 (= S165) mutation to A: Loss of activity.
- S218 (= S166) mutation to A: Lowers activity by at least 98%.
- D237 (= D185) mutation D->E,N: Loss of activity.
- S241 (= S189) mutation to A: Loss of activity.
- C249 (= C197) mutation to A: Loss of activity.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
34% identity, 38% coverage: 23:209/498 of query aligns to 6:194/457 of 6c6gA
Sites not aligning to the query:
3pr0A Crystal structure of a covalently bound alpha-ketoheterocycle inhibitor (phenhexyl/oxadiazole/pyridine) to a humanized variant of fatty acid amide hydrolase (see paper)
26% identity, 71% coverage: 81:436/498 of query aligns to 101:477/545 of 3pr0A
- active site: K110 (= K90), S185 (= S165), S186 (= S166), T204 (≠ N184), I206 (≠ G186), G207 (= G187), G208 (= G188), S209 (= S189), F212 (≠ I192)
- binding 7-phenyl-1-[5-(pyridin-2-yl)-1,3,4-oxadiazol-2-yl]heptane-1,1-diol: M159 (≠ G139), F160 (= F140), S161 (≠ N141), S185 (= S165), D205 (= D185), I206 (≠ G186), G207 (= G187), S209 (= S189), T456 (≠ R415)
3lj7A 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with carbamate inhibitor urb597 (see paper)
26% identity, 71% coverage: 81:436/498 of query aligns to 101:477/545 of 3lj7A
- active site: K110 (= K90), S185 (= S165), S186 (= S166), T204 (≠ N184), I206 (≠ G186), G207 (= G187), G208 (= G188), S209 (= S189), F212 (≠ I192)
- binding cyclohexane aminocarboxylic acid: F160 (= F140), I206 (≠ G186), G207 (= G187), S209 (= S189)
3k83B Crystal structure analysis of a biphenyl/oxazole/carboxypyridine alpha-ketoheterocycle inhibitor bound to a humanized variant of fatty acid amide hydrolase (see paper)
26% identity, 71% coverage: 81:436/498 of query aligns to 101:477/545 of 3k83B
- active site: K110 (= K90), S185 (= S165), S186 (= S166), T204 (≠ N184), I206 (≠ G186), G207 (= G187), G208 (= G188), S209 (= S189), F212 (≠ I192)
- binding 1-dodecanol: S114 (≠ N94), S132 (≠ A112), K235 (vs. gap)
- binding 6-[2-(3-biphenyl-4-ylpropanoyl)-1,3-oxazol-5-yl]pyridine-2-carboxylic acid: M159 (≠ G139), F160 (= F140), S161 (≠ N141), S185 (= S165), D205 (= D185), I206 (≠ G186), G207 (= G187), S209 (= S189), G236 (vs. gap), C237 (vs. gap), V238 (≠ I210), T456 (≠ R415)
3ppmA Crystal structure of a noncovalently bound alpha-ketoheterocycle inhibitor (phenhexyl/oxadiazole/pyridine) to a humanized variant of fatty acid amide hydrolase (see paper)
26% identity, 71% coverage: 81:436/498 of query aligns to 101:477/546 of 3ppmA
- active site: K110 (= K90), S185 (= S165), S186 (= S166), T204 (≠ N184), I206 (≠ G186), G207 (= G187), G208 (= G188), S209 (= S189), F212 (≠ I192)
- binding fluoride ion: D205 (= D185), I206 (≠ G186), G207 (= G187), S209 (= S189)
- binding 7-phenyl-1-[5-(pyridin-2-yl)-1,3,4-oxadiazol-2-yl]heptan-1-one: M159 (≠ G139), F160 (= F140), S185 (= S165), T204 (≠ N184), I206 (≠ G186), S209 (= S189), G236 (vs. gap), L246 (= L218), T456 (≠ R415), M463 (≠ P422)
3k84A Crystal structure analysis of a oleyl/oxadiazole/pyridine inhibitor bound to a humanized variant of fatty acid amide hydrolase (see paper)
26% identity, 71% coverage: 81:436/498 of query aligns to 101:477/546 of 3k84A
- active site: K110 (= K90), S185 (= S165), S186 (= S166), T204 (≠ N184), I206 (≠ G186), G207 (= G187), G208 (= G188), S209 (= S189), F212 (≠ I192)
- binding (9Z)-1-(5-pyridin-2-yl-1,3,4-oxadiazol-2-yl)octadec-9-en-1-one: M159 (≠ G139), F160 (= F140), S161 (≠ N141), S185 (= S165), T204 (≠ N184), I206 (≠ G186), G207 (= G187), S209 (= S189), T345 (≠ F325), T456 (≠ R415)
Sites not aligning to the query:
Query Sequence
>GFF1044 FitnessBrowser__Marino:GFF1044
MSAPQSCHSFRNDAIGCDDATALAERVRRREISVTELTQTAIARAQAVEPLLHGLASANY
DQAIRTASKLDAADQTGSFPLFRGVPTLIKDNTNVSGMTTRHGSLAVPSVPASDTSPFAR
QLLAQGFLCLGKSTLPEFGFNATTEPAHAPATCNPWNLAYSSGASSGGSAALVAAGVVPI
AHANDGGGSIRIPAACCGLVGLKPTRGRLIDNEAAASLPINIISEGVVTRSVRDTANFFE
QAETYFRNPGLPAIGKMEGPSGRPLRIGLVLDSINGHKTDDITRRTVEETALRLEKMGHR
IEPVPVPVHSTFPDDFALYWALLAFGIRANGRKLLHPAFDKHKTDGLTNGLDRMFRRQFW
RLPTALWRLKRSWHDYAHAMAGFDAVLTPVLGHTTPALGHLSPAVPFDTLFERLREYVSF
TPLANATGAPAISLPMGHTPDQLPVSVQFMGRHGGERTLLDIAFTLEANHPWPLLCDFNR
NNLGSREQNTRDSLANPV
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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