SitesBLAST
Comparing AZOBR_RS31530 FitnessBrowser__azobra:AZOBR_RS31530 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)
31% identity, 93% coverage: 16:446/462 of query aligns to 15:473/485 of 2f2aA
- active site: K79 (= K80), S154 (= S156), S155 (= S157), S173 (= S175), T175 (= T177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ L183)
- binding glutamine: G130 (= G132), S154 (= S156), D174 (= D176), T175 (= T177), G176 (= G178), S178 (= S180), F206 (≠ L208), Y309 (vs. gap), Y310 (vs. gap), R358 (= R329), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
31% identity, 93% coverage: 16:446/462 of query aligns to 15:473/485 of 2dqnA
- active site: K79 (= K80), S154 (= S156), S155 (= S157), S173 (= S175), T175 (= T177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ L183)
- binding asparagine: M129 (= M131), G130 (= G132), T175 (= T177), G176 (= G178), S178 (= S180), Y309 (vs. gap), Y310 (vs. gap), R358 (= R329), D425 (vs. gap)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 98% coverage: 8:458/462 of query aligns to 6:478/478 of 3h0mA
- active site: K72 (= K80), S147 (= S156), S148 (= S157), S166 (= S175), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ L183)
- binding glutamine: M122 (= M131), G123 (= G132), D167 (= D176), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), F199 (≠ L208), Y302 (≠ N300), R351 (= R329), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 98% coverage: 8:458/462 of query aligns to 6:478/478 of 3h0lA
- active site: K72 (= K80), S147 (= S156), S148 (= S157), S166 (= S175), T168 (= T177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ L183)
- binding asparagine: G123 (= G132), S147 (= S156), G169 (= G178), G170 (= G179), S171 (= S180), Y302 (≠ N300), R351 (= R329), D418 (vs. gap)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
37% identity, 94% coverage: 7:440/462 of query aligns to 1:442/457 of 6c6gA
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, 88% coverage: 44:449/462 of query aligns to 169:591/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 156:157) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 177:180) binding
- S305 (= S180) mutation to A: Loss of activity.
- R307 (= R182) mutation to A: Loss of activity.
- S360 (≠ R235) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 88% coverage: 44:449/462 of query aligns to 169:591/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A130), T258 (≠ P133), S281 (= S156), G302 (≠ T177), G303 (= G178), S305 (= S180), S472 (≠ R327), I532 (≠ A390), M539 (≠ A397)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
34% identity, 96% coverage: 7:450/462 of query aligns to 28:491/507 of Q84DC4
- T31 (= T10) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K80) mutation to A: Abolishes activity on mandelamide.
- S180 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G178) 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 (= S180) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ L183) 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 (vs. gap) 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 (≠ A349) 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 (≠ T400) 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.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 93% coverage: 19:447/462 of query aligns to 18:477/487 of 1m21A
- active site: K81 (= K80), S160 (= S156), S161 (= S157), T179 (≠ S175), T181 (= T177), D182 (≠ G178), G183 (= G179), S184 (= S180), C187 (≠ L183)
- binding : A129 (= A130), N130 (≠ M131), F131 (vs. gap), C158 (≠ G154), G159 (= G155), S160 (= S156), S184 (= S180), C187 (≠ L183), I212 (≠ L208), R318 (≠ N300), L321 (≠ F303), L365 (= L334), F426 (≠ G384)
3kfuE Crystal structure of the transamidosome (see paper)
36% identity, 92% coverage: 26:448/462 of query aligns to 19:456/468 of 3kfuE
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
33% identity, 82% coverage: 70:450/462 of query aligns to 85:501/508 of 3a1iA
- active site: K95 (= K80), S170 (= S156), S171 (= S157), G189 (≠ S175), Q191 (≠ T177), G192 (= G178), G193 (= G179), A194 (≠ S180), I197 (≠ L183)
- binding benzamide: F145 (≠ M131), S146 (≠ G132), G147 (≠ P133), Q191 (≠ T177), G192 (= G178), G193 (= G179), A194 (≠ S180), W327 (vs. gap)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
34% identity, 92% coverage: 24:447/462 of query aligns to 19:439/461 of 4gysB
- active site: K72 (= K80), S146 (= S156), S147 (= S157), T165 (≠ S175), T167 (= T177), A168 (≠ G178), G169 (= G179), S170 (= S180), V173 (≠ L183)
- binding malonate ion: A120 (= A130), G122 (= G132), S146 (= S156), T167 (= T177), A168 (≠ G178), S170 (= S180), S193 (≠ D203), G194 (= G204), V195 (= V205), R200 (≠ E210), Y297 (≠ F303), R305 (= R318)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 97% coverage: 3:449/462 of query aligns to 1:447/457 of 5h6sC
- active site: K77 (= K80), S152 (= S156), S153 (= S157), L173 (≠ T177), G174 (= G178), G175 (= G179), S176 (= S180)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A130), R128 (≠ G132), W129 (≠ P133), S152 (= S156), L173 (≠ T177), G174 (= G178), S176 (= S180), W306 (≠ L298), F338 (≠ Y322)
Q9FR37 Amidase 1; AtAMI1; Translocon at the outer membrane of chloroplasts 64-I; AtTOC64-I; EC 3.5.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
46% identity, 34% coverage: 72:228/462 of query aligns to 28:182/425 of Q9FR37
- K36 (= K80) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S156) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S157) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D176) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S180) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C188) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 90% coverage: 28:445/462 of query aligns to 37:460/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (= S156) mutation to A: Loss of activity.
- S189 (= S180) 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)
31% identity, 62% coverage: 5:290/462 of query aligns to 3:341/564 of 6te4A
Sites not aligning to the query:
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
26% identity, 95% coverage: 11:451/462 of query aligns to 10:478/490 of 4yjiA
- active site: K79 (= K80), S158 (= S156), S159 (= S157), G179 (≠ T177), G180 (= G178), G181 (= G179), A182 (≠ S180)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ M82), G132 (≠ A130), S158 (= S156), G179 (≠ T177), G180 (= G178), A182 (≠ S180)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
31% identity, 78% coverage: 70:431/462 of query aligns to 52:392/412 of 1ocmA
- active site: K62 (= K80), S131 (= S156), S132 (= S157), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180)
- binding pyrophosphate 2-: R113 (vs. gap), S131 (= S156), Q151 (≠ D176), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ L183), P359 (≠ A397)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
31% identity, 78% coverage: 70:431/462 of query aligns to 52:392/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S156), S132 (= S157), T150 (≠ S175), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ L183)
- binding 3-amino-3-oxopropanoic acid: G130 (= G155), T152 (= T177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ L183), P359 (≠ A397)
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
26% identity, 79% coverage: 77:439/462 of query aligns to 66:444/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
Query Sequence
>AZOBR_RS31530 FitnessBrowser__azobra:AZOBR_RS31530
MTDPTSLTLTEAARAVRDGTLRAEALADACLDRIARLNPTLNAFLSVEPEEALAAARAAD
AEVRAGRLRGPLHGVPLAHKDMFHRAGKRCTCGSPTIRGDFRPERTATVLERLDTAGAVT
LGTLHMAEFAMGPTGHNAHLGRCRNPWDPDRITGGSSSGSGAAVAGRLAFGSLGSDTGGS
VRLPAALCGVVGLKPTQGATPMDGVMPLSESLDCVGPLARSAEDAATLFSVITGRTDAVA
AIGQGVEGLRLGIPRQFYYDGLDPAVAAALERARAVLERAGARVVDVDIPDHEPYGDLAN
LVFTPEAAAVHAPWLRERPQDYGPQVRARLLQGLMVPAASYLQAKQLRALHLRAMIDGPF
ARCDALFVPALRSRVPTAAQTDVGAGPAMAAVVAGVAALTRPVSYLGLPALVTPAGFDPD
GMPIAMQLIARPQAEATLLRIADAYERAAGWLSRVPQTQVFS
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