SitesBLAST
Comparing Ga0059261_0082 FitnessBrowser__Korea:Ga0059261_0082 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
50% identity, 90% coverage: 40:483/494 of query aligns to 40:475/485 of 2f2aA
- active site: K79 (= K79), S154 (= S160), S155 (= S161), S173 (≠ T179), T175 (= T181), G176 (= G182), G177 (= G183), S178 (= S184), Q181 (= Q187)
- binding glutamine: G130 (= G130), S154 (= S160), D174 (= D180), T175 (= T181), G176 (= G182), S178 (= S184), F206 (= F212), Y309 (= Y315), Y310 (= Y316), R358 (= R365), D425 (= D432)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
50% identity, 90% coverage: 40:483/494 of query aligns to 40:475/485 of 2dqnA
- active site: K79 (= K79), S154 (= S160), S155 (= S161), S173 (≠ T179), T175 (= T181), G176 (= G182), G177 (= G183), S178 (= S184), Q181 (= Q187)
- binding asparagine: M129 (= M129), G130 (= G130), T175 (= T181), G176 (= G182), S178 (= S184), Y309 (= Y315), Y310 (= Y316), R358 (= R365), D425 (= D432)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 96% coverage: 9:483/494 of query aligns to 7:468/478 of 3h0mA
- active site: K72 (= K79), S147 (= S160), S148 (= S161), S166 (≠ T179), T168 (= T181), G169 (= G182), G170 (= G183), S171 (= S184), Q174 (= Q187)
- binding glutamine: M122 (= M129), G123 (= G130), D167 (= D180), T168 (= T181), G169 (= G182), G170 (= G183), S171 (= S184), F199 (= F212), Y302 (= Y315), R351 (= R365), D418 (= D432)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 96% coverage: 9:483/494 of query aligns to 7:468/478 of 3h0lA
- active site: K72 (= K79), S147 (= S160), S148 (= S161), S166 (≠ T179), T168 (= T181), G169 (= G182), G170 (= G183), S171 (= S184), Q174 (= Q187)
- binding asparagine: G123 (= G130), S147 (= S160), G169 (= G182), G170 (= G183), S171 (= S184), Y302 (= Y315), R351 (= R365), D418 (= D432)
3kfuE Crystal structure of the transamidosome (see paper)
46% identity, 95% coverage: 12:482/494 of query aligns to 5:455/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
38% identity, 82% coverage: 71:475/494 of query aligns to 30:444/450 of 4n0iA
- active site: K38 (= K79), S116 (= S160), S117 (= S161), T135 (= T179), T137 (= T181), G138 (= G182), G139 (= G183), S140 (= S184), L143 (≠ Q187)
- binding glutamine: G89 (= G130), T137 (= T181), G138 (= G182), S140 (= S184), Y168 (≠ F212), Y271 (= Y315), Y272 (= Y316), R320 (= R365), D404 (= D432)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 96% coverage: 9:483/494 of query aligns to 8:478/487 of 1m21A
- active site: K81 (= K79), S160 (= S160), S161 (= S161), T179 (= T179), T181 (= T181), D182 (≠ G182), G183 (= G183), S184 (= S184), C187 (≠ Q187)
- binding : A129 (= A128), N130 (≠ M129), F131 (≠ G130), C158 (≠ G158), G159 (= G159), S160 (= S160), S184 (= S184), C187 (≠ Q187), I212 (≠ F212), R318 (≠ Y316), L321 (≠ A319), L365 (= L367), F426 (≠ Y429)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 95% coverage: 12:481/494 of query aligns to 6:448/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 85% coverage: 71:492/494 of query aligns to 87:508/508 of 3a1iA
- active site: K95 (= K79), S170 (≠ A154), S171 (≠ L155), G189 (≠ T179), Q191 (≠ T181), G192 (= G182), G193 (= G183), A194 (≠ S184), I197 (≠ Q187)
- binding benzamide: F145 (≠ M129), S146 (≠ G130), G147 (≠ S131), Q191 (≠ T181), G192 (= G182), G193 (= G183), A194 (≠ S184), W327 (≠ Y315)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 97% coverage: 16:492/494 of query aligns to 37:498/507 of Q84DC4
- K100 (= K79) mutation to A: Abolishes activity on mandelamide.
- S180 (= S160) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S161) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G182) 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 (= S184) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q187) 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 (= S304) 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 (≠ D379) 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 (≠ L430) 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.
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, 98% coverage: 12:494/494 of query aligns to 131:601/607 of Q7XJJ7
- K205 (= K79) mutation to A: Loss of activity.
- SS 281:282 (= SS 160:161) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 181:184) binding
- S305 (= S184) mutation to A: Loss of activity.
- R307 (= R186) mutation to A: Loss of activity.
- S360 (≠ F239) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 98% coverage: 12:494/494 of query aligns to 131:601/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A128), T258 (≠ S131), S281 (= S160), G302 (≠ T181), G303 (= G182), S305 (= S184), S472 (≠ A356), I532 (≠ A423), M539 (≠ L430)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 86% coverage: 49:473/494 of query aligns to 62:453/605 of Q936X2
- K91 (= K79) mutation to A: Loss of activity.
- S165 (= S160) mutation to A: Loss of activity.
- S189 (= S184) mutation to A: Loss of activity.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 96% coverage: 10:482/494 of query aligns to 9:474/490 of 4yjiA
- active site: K79 (= K79), S158 (= S160), S159 (= S161), G179 (≠ T181), G180 (= G182), G181 (= G183), A182 (≠ S184)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L81), G132 (≠ A128), S158 (= S160), G179 (≠ T181), G180 (= G182), A182 (≠ S184)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 86% coverage: 49:473/494 of query aligns to 45:430/461 of 4gysB
- active site: K72 (= K79), S146 (≠ P157), S147 (≠ G158), T165 (= T179), T167 (= T181), A168 (≠ G182), G169 (= G183), S170 (= S184), V173 (≠ Q187)
- binding malonate ion: A120 (= A128), G122 (= G130), S146 (≠ P157), T167 (= T181), A168 (≠ G182), S170 (= S184), S193 (≠ W207), G194 (= G208), V195 (= V209), R200 (≠ S214), Y297 (= Y330), R305 (= R338)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
29% identity, 62% coverage: 3:306/494 of query aligns to 1:341/564 of 6te4A
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 98% coverage: 3:484/494 of query aligns to 1:447/457 of 5h6sC
- active site: K77 (= K79), S152 (= S160), S153 (= S161), L173 (≠ T181), G174 (= G182), G175 (= G183), S176 (= S184)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A128), R128 (≠ G130), W129 (≠ S131), S152 (= S160), L173 (≠ T181), G174 (= G182), S176 (= S184), W306 (≠ Y316), F338 (≠ I368)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
33% identity, 51% coverage: 16:269/494 of query aligns to 14:259/482 of 3a2qA
- active site: K69 (= K79), S147 (= S160), S148 (= S161), N166 (≠ T179), A168 (≠ T181), A169 (≠ G182), G170 (= G183), A171 (≠ S184), I174 (≠ Q187)
- binding 6-aminohexanoic acid: G121 (≠ A128), G121 (≠ A128), N122 (≠ M129), S147 (= S160), A168 (≠ T181), A168 (≠ T181), A169 (≠ G182), A171 (≠ S184)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
25% identity, 93% coverage: 7:466/494 of query aligns to 2:392/412 of 1o9oA
- active site: K62 (= K79), A131 (≠ S160), S132 (= S161), T150 (= T179), T152 (= T181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ Q187)
- binding 3-amino-3-oxopropanoic acid: G130 (= G159), T152 (= T181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ Q187), P359 (= P425)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
26% identity, 85% coverage: 46:466/494 of query aligns to 33:392/412 of 1ocmA
- active site: K62 (= K79), S131 (= S160), S132 (= S161), T152 (= T181), G153 (= G182), G154 (= G183), S155 (= S184)
- binding pyrophosphate 2-: R113 (≠ S132), S131 (= S160), Q151 (≠ D180), T152 (= T181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ Q187), P359 (= P425)
Query Sequence
>Ga0059261_0082 FitnessBrowser__Korea:Ga0059261_0082
MTDVTTLGVAAIRDGVRSGEFTAIEVADAFITKVSAAKQLNAFIVETPDHAIAAARTADA
ARAAGETLKPLAGVPIGMKDLFCTKGVQTTAASHMLEGFTPVYESTVSQKLWDAGAGMLG
KLNLDQFAMGSSNETSYFGNVISPWRRKDGGNAALAPGGSSGGSSSAIAARLVPAATGTD
TGGSIRQPAAFTGISGIKPTYGRCSRWGVVAFASSLDQAGPMARDVRDCAIMLEAMAGFD
PKDATSLDMAVPNWEAGLSADLRGKKVGIPKEYRVDGMPAEIEALWQQGIDWLKDAGAEI
VEVSLPHTKYALPAYYIIAPAEASSNLARYDGVRYGQRDLPDGANLQEMYAATRAAGFGP
EVQRRILIGTYVLSAGFYDAYYTQAQKVRTLIAQDFEKAWAQCDLLLTPTAPSAAFALGE
KSADPLAMYLNDVFTVPSSLAGIPAMSVPGGLDKDGLPLGLQIIGKPFDEQGVLNASLAI
EQRAGFTAKPEQWW
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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