SitesBLAST
Comparing AZOBR_RS20645 FitnessBrowser__azobra:AZOBR_RS20645 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)
51% identity, 91% coverage: 33:480/493 of query aligns to 32:473/485 of 2f2aA
- active site: K79 (= K78), S154 (= S161), S155 (= S162), S173 (≠ T180), T175 (= T182), G176 (= G183), G177 (= G184), S178 (= S185), Q181 (= Q188)
- binding glutamine: G130 (= G129), S154 (= S161), D174 (= D181), T175 (= T182), G176 (= G183), S178 (= S185), F206 (= F213), Y309 (= Y316), Y310 (= Y317), R358 (= R364), D425 (= D431)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
51% identity, 91% coverage: 33:480/493 of query aligns to 32:473/485 of 2dqnA
- active site: K79 (= K78), S154 (= S161), S155 (= S162), S173 (≠ T180), T175 (= T182), G176 (= G183), G177 (= G184), S178 (= S185), Q181 (= Q188)
- binding asparagine: M129 (= M128), G130 (= G129), T175 (= T182), G176 (= G183), S178 (= S185), Y309 (= Y316), Y310 (= Y317), R358 (= R364), D425 (= D431)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 96% coverage: 8:481/493 of query aligns to 6:467/478 of 3h0mA
- active site: K72 (= K78), S147 (= S161), S148 (= S162), S166 (≠ T180), T168 (= T182), G169 (= G183), G170 (= G184), S171 (= S185), Q174 (= Q188)
- binding glutamine: M122 (= M128), G123 (= G129), D167 (= D181), T168 (= T182), G169 (= G183), G170 (= G184), S171 (= S185), F199 (= F213), Y302 (= Y316), R351 (= R364), D418 (= D431)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 96% coverage: 8:481/493 of query aligns to 6:467/478 of 3h0lA
- active site: K72 (= K78), S147 (= S161), S148 (= S162), S166 (≠ T180), T168 (= T182), G169 (= G183), G170 (= G184), S171 (= S185), Q174 (= Q188)
- binding asparagine: G123 (= G129), S147 (= S161), G169 (= G183), G170 (= G184), S171 (= S185), Y302 (= Y316), R351 (= R364), D418 (= D431)
3kfuE Crystal structure of the transamidosome (see paper)
46% identity, 95% coverage: 16:484/493 of query aligns to 9:458/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
39% identity, 82% coverage: 70:473/493 of query aligns to 30:443/450 of 4n0iA
- active site: K38 (= K78), S116 (= S161), S117 (= S162), T135 (= T180), T137 (= T182), G138 (= G183), G139 (= G184), S140 (= S185), L143 (≠ Q188)
- binding glutamine: G89 (= G129), T137 (= T182), G138 (= G183), S140 (= S185), Y168 (≠ F213), Y271 (= Y316), Y272 (= Y317), R320 (= R364), D404 (= D431)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
32% identity, 97% coverage: 13:489/493 of query aligns to 43:506/508 of 3a1iA
- active site: K95 (= K78), S170 (= S161), S171 (= S162), G189 (≠ T180), Q191 (≠ T182), G192 (= G183), G193 (= G184), A194 (≠ S185), I197 (≠ Q188)
- binding benzamide: F145 (≠ M128), S146 (≠ G129), G147 (≠ S130), Q191 (≠ T182), G192 (= G183), G193 (= G184), A194 (≠ S185), W327 (≠ Y316)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 96% coverage: 20:491/493 of query aligns to 19:487/487 of 1m21A
- active site: K81 (= K78), S160 (= S161), S161 (= S162), T179 (= T180), T181 (= T182), D182 (≠ G183), G183 (= G184), S184 (= S185), C187 (≠ Q188)
- binding : A129 (= A127), N130 (≠ M128), F131 (≠ G129), C158 (≠ G159), G159 (= G160), S160 (= S161), S184 (= S185), C187 (≠ Q188), I212 (≠ F213), R318 (≠ Y317), L321 (≠ A320), L365 (= L366), F426 (vs. gap)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 95% coverage: 13:480/493 of query aligns to 7:448/457 of 6c6gA
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 89% coverage: 49:489/493 of query aligns to 175:597/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A127), T258 (≠ S130), S281 (= S161), G302 (≠ T182), G303 (= G183), S305 (= S185), S472 (≠ T369), I532 (= I425), M539 (≠ V432)
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, 89% coverage: 49:489/493 of query aligns to 175:597/607 of Q7XJJ7
- K205 (= K78) mutation to A: Loss of activity.
- SS 281:282 (= SS 161:162) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 182:185) binding
- S305 (= S185) mutation to A: Loss of activity.
- R307 (= R187) mutation to A: Loss of activity.
- S360 (≠ F240) mutation to A: No effect.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 98% coverage: 7:489/493 of query aligns to 30:496/507 of Q84DC4
- T31 (= T8) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K78) mutation to A: Abolishes activity on mandelamide.
- S180 (= S161) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S162) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G183) 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 (= S185) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q188) 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 (≠ K295) 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 (≠ D378) 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 (≠ Y428) 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.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 90% coverage: 49:490/493 of query aligns to 62:476/605 of Q936X2
- K91 (= K78) mutation to A: Loss of activity.
- S165 (= S153) mutation to A: Loss of activity.
- S189 (= S185) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 88% coverage: 49:481/493 of query aligns to 45:439/461 of 4gysB
- active site: K72 (= K78), S146 (= S161), S147 (= S162), T165 (= T180), T167 (= T182), A168 (≠ G183), G169 (= G184), S170 (= S185), V173 (≠ Q188)
- binding malonate ion: A120 (= A127), G122 (= G129), S146 (= S161), T167 (= T182), A168 (≠ G183), S170 (= S185), S193 (≠ W208), G194 (= G209), V195 (= V210), R200 (≠ S215), Y297 (= Y331), R305 (= R339)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 95% coverage: 14:483/493 of query aligns to 16:447/457 of 5h6sC
- active site: K77 (= K78), S152 (= S161), S153 (= S162), L173 (≠ T182), G174 (= G183), G175 (= G184), S176 (= S185)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A127), R128 (≠ G129), W129 (≠ S130), S152 (= S161), L173 (≠ T182), G174 (= G183), S176 (= S185), W306 (≠ Y316), F338 (≠ I367)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
27% identity, 97% coverage: 5:483/493 of query aligns to 3:476/490 of 4yjiA
- active site: K79 (= K78), S158 (= S161), S159 (= S162), G179 (≠ T182), G180 (= G183), G181 (= G184), A182 (≠ S185)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L80), G132 (≠ A127), S158 (= S161), G179 (≠ T182), G180 (= G183), A182 (≠ S185)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
28% identity, 62% coverage: 4:307/493 of query aligns to 2:341/564 of 6te4A
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 90% coverage: 41:484/493 of query aligns to 26:411/412 of 1o9oA
- active site: K62 (= K78), A131 (≠ S161), S132 (= S162), T150 (= T180), T152 (= T182), G153 (= G183), G154 (= G184), S155 (= S185), R158 (≠ Q188)
- binding 3-amino-3-oxopropanoic acid: G130 (= G160), T152 (= T182), G153 (= G183), G154 (= G184), S155 (= S185), R158 (≠ Q188), P359 (= P424)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
26% identity, 90% coverage: 41:484/493 of query aligns to 26:411/412 of 1ocmA
- active site: K62 (= K78), S131 (≠ I156), S132 (≠ V157), T152 (= T182), G153 (= G183), G154 (= G184), S155 (= S185)
- binding pyrophosphate 2-: R113 (≠ G129), S131 (≠ I156), Q151 (≠ D181), T152 (= T182), G153 (= G183), G154 (= G184), S155 (= S185), R158 (≠ Q188), P359 (= P424)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
29% identity, 51% coverage: 20:270/493 of query aligns to 18:259/482 of 3a2qA
- active site: K69 (= K78), S147 (= S161), S148 (= S162), N166 (≠ T180), A168 (≠ T182), A169 (≠ G183), G170 (= G184), A171 (≠ S185), I174 (≠ Q188)
- binding 6-aminohexanoic acid: G121 (≠ A127), G121 (≠ A127), N122 (≠ M128), S147 (= S161), A168 (≠ T182), A168 (≠ T182), A169 (≠ G183), A171 (≠ S185)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS20645 FitnessBrowser__azobra:AZOBR_RS20645
MTGLTHLTMAAALDGLAKKEFTAVELTEAHVKAVETIRPLNAFITETPEQALAMAKASDA
RRAKGEAGPMEGLPIAVKDLFCTKGVPTTAASHILDGFKPEYESTVTSNLWRDGAVMLGK
VNLDEFAMGSANITSHHGNVISPWSPGEVGNWSRQIVPGGSSGGSAAAVAARAALGATGT
DTGGSIRQPAAFTGIVGIKPTYGRCSRWGVVAFASSLDQAGPMTRTVEDAAIMLRSMCGF
DPKDSTSVDLPVPDFRAALTGDIRGLKVGIPKEYRVEGMPAEIAAIWDQGIEWLKQAGAE
PVEISLPHTKYALATYYIVAPAEASSNLARYDGLRYGLRVEGASLKDMYENTRGAGFGKE
VRRRILIGTYVLSAGYYDAYYNKARQVRTRIKWDFDEAFKQCDVILTPTAPSTAFAIGEK
MDDPIQMYLNDVFTVPASLAGLPGMSVPAGVGSDGLPLGLQLLGRPFDEETVLRVGQVIE
KAAAVTATPPFMA
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