SitesBLAST
Comparing AZOBR_RS22825 FitnessBrowser__azobra:AZOBR_RS22825 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)
3kfuE Crystal structure of the transamidosome (see paper)
38% identity, 98% coverage: 3:456/463 of query aligns to 2:458/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 98% coverage: 2:454/463 of query aligns to 7:474/485 of 2f2aA
- active site: K79 (= K73), S154 (= S148), S155 (= S149), S173 (≠ T167), T175 (≠ G169), G176 (= G170), G177 (= G171), S178 (= S172), Q181 (≠ R175)
- binding glutamine: G130 (≠ K124), S154 (= S148), D174 (= D168), T175 (≠ G169), G176 (= G170), S178 (= S172), F206 (= F203), Y309 (≠ V296), Y310 (≠ W297), R358 (≠ Q336), D425 (≠ A403)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 98% coverage: 2:454/463 of query aligns to 7:474/485 of 2dqnA
- active site: K79 (= K73), S154 (= S148), S155 (= S149), S173 (≠ T167), T175 (≠ G169), G176 (= G170), G177 (= G171), S178 (= S172), Q181 (≠ R175)
- binding asparagine: M129 (≠ C123), G130 (≠ K124), T175 (≠ G169), G176 (= G170), S178 (= S172), Y309 (≠ V296), Y310 (≠ W297), R358 (≠ Q336), D425 (≠ A403)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 98% coverage: 2:453/463 of query aligns to 6:466/478 of 3h0mA
- active site: K72 (= K73), S147 (= S148), S148 (= S149), S166 (≠ T167), T168 (≠ G169), G169 (= G170), G170 (= G171), S171 (= S172), Q174 (≠ R175)
- binding glutamine: M122 (≠ C123), G123 (≠ K124), D167 (= D168), T168 (≠ G169), G169 (= G170), G170 (= G171), S171 (= S172), F199 (= F198), Y302 (≠ W297), R351 (≠ Q336), D418 (≠ A403)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 98% coverage: 2:453/463 of query aligns to 6:466/478 of 3h0lA
- active site: K72 (= K73), S147 (= S148), S148 (= S149), S166 (≠ T167), T168 (≠ G169), G169 (= G170), G170 (= G171), S171 (= S172), Q174 (≠ R175)
- binding asparagine: G123 (≠ K124), S147 (= S148), G169 (= G170), G170 (= G171), S171 (= S172), Y302 (≠ W297), R351 (≠ Q336), D418 (≠ A403)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
32% identity, 98% coverage: 2:453/463 of query aligns to 7:473/490 of 4yjiA
- active site: K79 (= K73), S158 (= S148), S159 (= S149), G179 (= G169), G180 (= G170), G181 (= G171), A182 (≠ S172)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N75), G132 (≠ A122), S158 (= S148), G179 (= G169), G180 (= G170), A182 (≠ S172)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
34% identity, 86% coverage: 65:460/463 of query aligns to 87:504/508 of 3a1iA
- active site: K95 (= K73), S170 (= S148), S171 (= S149), G189 (≠ T167), Q191 (≠ G169), G192 (= G170), G193 (= G171), A194 (≠ S172), I197 (≠ R175)
- binding benzamide: F145 (≠ C123), S146 (≠ K124), G147 (= G125), Q191 (≠ G169), G192 (= G170), G193 (= G171), A194 (≠ S172), W327 (vs. gap)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 96% coverage: 9:453/463 of query aligns to 14:476/487 of 1m21A
- active site: K81 (= K73), S160 (= S148), S161 (= S149), T179 (= T167), T181 (≠ G169), D182 (≠ G170), G183 (= G171), S184 (= S172), C187 (≠ R175)
- binding : A129 (= A122), N130 (vs. gap), F131 (≠ C123), C158 (≠ G146), G159 (= G147), S160 (= S148), S184 (= S172), C187 (≠ R175), I212 (≠ P201), R318 (≠ S304), L321 (≠ M307), L365 (vs. gap), F426 (≠ R395)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 98% coverage: 1:455/463 of query aligns to 1:450/457 of 6c6gA
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 96% coverage: 1:446/463 of query aligns to 5:437/457 of 5h6sC
- active site: K77 (= K73), S152 (= S148), S153 (= S149), L173 (≠ G169), G174 (= G170), G175 (= G171), S176 (= S172)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A122), R128 (≠ K124), W129 (≠ G125), S152 (= S148), L173 (≠ G169), G174 (= G170), S176 (= S172), W306 (= W297), F338 (= F329)
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, 96% coverage: 9:453/463 of query aligns to 147:588/607 of Q7XJJ7
- K205 (= K73) mutation to A: Loss of activity.
- SS 281:282 (= SS 148:149) mutation to AA: Loss of activity.
- GGGS 302:305 (= GGGS 169:172) binding
- S305 (= S172) mutation to A: Loss of activity.
- R307 (= R174) mutation to A: Loss of activity.
- S360 (≠ P228) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 96% coverage: 9:453/463 of query aligns to 147:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A122), T258 (≠ G125), S281 (= S148), G302 (= G169), G303 (= G170), S305 (= S172), S472 (≠ G334), I532 (≠ G394), M539 (≠ G401)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
33% identity, 95% coverage: 8:449/463 of query aligns to 19:434/461 of 4gysB
- active site: K72 (= K73), S146 (= S148), S147 (= S149), T165 (= T167), T167 (≠ G169), A168 (≠ G170), G169 (= G171), S170 (= S172), V173 (≠ R175)
- binding malonate ion: A120 (= A122), G122 (≠ K124), S146 (= S148), T167 (≠ G169), A168 (≠ G170), S170 (= S172), S193 (≠ P195), G194 (= G197), V195 (≠ F198), R200 (≠ F203), Y297 (≠ G305), R305 (≠ G313)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
30% identity, 97% coverage: 7:453/463 of query aligns to 11:468/482 of 3a2qA
- active site: K69 (= K73), S147 (= S148), S148 (= S149), N166 (≠ T167), A168 (≠ G169), A169 (≠ G170), G170 (= G171), A171 (≠ S172), I174 (≠ R175)
- binding 6-aminohexanoic acid: G121 (≠ A122), G121 (≠ A122), N122 (≠ C123), S147 (= S148), A168 (≠ G169), A168 (≠ G169), A169 (≠ G170), A171 (≠ S172), C313 (vs. gap)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 97% coverage: 10:460/463 of query aligns to 37:494/507 of Q84DC4
- K100 (= K73) mutation to A: Abolishes activity on mandelamide.
- S180 (= S148) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S149) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G170) 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 (= S172) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ R175) 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 (≠ G302) 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 (≠ V348) 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 (≠ L408) 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.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 93% coverage: 23:453/463 of query aligns to 41:462/605 of Q936X2
- K91 (= K73) mutation to A: Loss of activity.
- S165 (= S148) mutation to A: Loss of activity.
- S189 (= S172) mutation to A: Loss of activity.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
38% identity, 47% coverage: 15:230/463 of query aligns to 19:241/564 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, 93% coverage: 23:453/463 of query aligns to 6:407/412 of 1o9oA
- active site: K62 (= K73), A131 (≠ S148), S132 (= S149), T150 (= T167), T152 (≠ G169), G153 (= G170), G154 (= G171), S155 (= S172), R158 (= R175)
- binding 3-amino-3-oxopropanoic acid: G130 (= G147), T152 (≠ G169), G153 (= G170), G154 (= G171), S155 (= S172), R158 (= R175), P359 (= P399)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 93% coverage: 23:453/463 of query aligns to 6:407/412 of 1ocmA
- active site: K62 (= K73), S131 (= S148), S132 (= S149), T152 (≠ G169), G153 (= G170), G154 (= G171), S155 (= S172)
- binding pyrophosphate 2-: R113 (≠ K124), S131 (= S148), Q151 (≠ D168), T152 (≠ G169), G153 (= G170), G154 (= G171), S155 (= S172), R158 (= R175), P359 (= P399)
1mt5A Crystal structure of fatty acid amide hydrolase (see paper)
35% identity, 33% coverage: 65:215/463 of query aligns to 98:251/537 of 1mt5A
- active site: K106 (= K73), S181 (= S148), S182 (= S149), T200 (= T167), I202 (≠ G169), G203 (= G170), G204 (= G171), S205 (= S172), F208 (≠ R175)
- binding methyl arachidonyl fluorophosphonate: M155 (≠ A122), L156 (≠ C123), S157 (≠ K124), S181 (= S148), D201 (= D168), I202 (≠ G169), G203 (= G170), S205 (= S172)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS22825 FitnessBrowser__azobra:AZOBR_RS22825
MSARRIAEQVAARAVSAVALYDDLLERIAAENPRLNAIVHLDPEAGRAEARAADARAARG
EALPLLGVPFTVKDNIWVRGQPVRQGSRLFQDFVGPEDAVAVARLRAAGAVFAGITNCSE
FACKGVTTNLLHGPTRNPWDVALTPGGSSGGAASAVAAGLAPLALCTDGGGSTRRPAAHV
GVVGMKPSAGVVPHPVGFAEPVFGNSVIGQMARSVGDVALMLDVLAGPDPRDPQSLPLSG
SFARAIANPDPAGLRIAYSRRLGLDAPVDPEVAACVERAVHRLADAGAIVEEADPVWPDG
AGESGLMPLQFAGLAALYGERYRATPDLFDPDIGQQIEAGLRTSGAEVARALHLREEAYR
ALAALFTRFDLLVCPTTPVTAWPFDRLGPATIDGRPVTPRGHAVFTPLFNHCYAPACSVP
CGLTESGGLPVGLQIAGPRLSDAAVLRLAAVVEATCGYTPPML
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