SitesBLAST
Comparing BWI76_RS07545 FitnessBrowser__Koxy:BWI76_RS07545 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)
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)
35% identity, 92% coverage: 24:387/394 of query aligns to 28:425/425 of Q9FR37
- K36 (= K32) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S109) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S110) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D129) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S133) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C141) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ P209) mutation to T: Slightly reduces catalytic activity.
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
31% identity, 91% coverage: 25:381/394 of query aligns to 62:445/593 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.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 92% coverage: 23:383/394 of query aligns to 91:483/507 of Q84DC4
- K100 (= K32) mutation to A: Abolishes activity on mandelamide.
- S180 (= S109) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S110) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G131) 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 (= S133) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ T136) 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 (≠ V230) 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 (= Q288) 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 (≠ S338) 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)
28% identity, 93% coverage: 24:388/394 of query aligns to 197:589/607 of Q7XJJ7
- K205 (= K32) mutation to A: Loss of activity.
- SS 281:282 (= SS 109:110) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 130:133) binding
- S305 (= S133) mutation to A: Loss of activity.
- R307 (= R135) mutation to A: Loss of activity.
- S360 (≠ D188) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 93% coverage: 24:388/394 of query aligns to 197:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A83), T258 (≠ M86), S281 (= S109), G302 (≠ T130), G303 (= G131), S305 (= S133), S472 (≠ R277), I532 (≠ R335), M539 (≠ L342)
Sites not aligning to the query:
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
39% identity, 43% coverage: 23:192/394 of query aligns to 72:243/487 of 1m21A
- active site: K81 (= K32), S160 (= S109), S161 (= S110), T179 (= T128), T181 (= T130), D182 (≠ G131), G183 (= G132), S184 (= S133), C187 (≠ T136)
- binding : A129 (= A83), N130 (≠ Y84), F131 (vs. gap), C158 (≠ G107), G159 (= G108), S160 (= S109), S184 (= S133), C187 (≠ T136), I212 (≠ L161)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 93% coverage: 19:383/394 of query aligns to 59:434/461 of 4gysB
- active site: K72 (= K32), S146 (= S109), S147 (= S110), T165 (= T128), T167 (= T130), A168 (≠ G131), G169 (= G132), S170 (= S133), V173 (≠ T136)
- binding malonate ion: A120 (= A83), G122 (≠ S85), S146 (= S109), T167 (= T130), A168 (≠ G131), S170 (= S133), S193 (≠ D156), G194 (= G157), V195 (≠ C158), R200 (≠ A163), Y297 (vs. gap), R305 (≠ A255)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
43% identity, 39% coverage: 23:176/394 of query aligns to 65:217/457 of 6c6gA
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 93% coverage: 20:386/394 of query aligns to 67:472/485 of 2f2aA
- active site: K79 (= K32), S154 (= S109), S155 (= S110), S173 (≠ T128), T175 (= T130), G176 (= G131), G177 (= G132), S178 (= S133), Q181 (≠ T136)
- binding glutamine: G130 (≠ S85), S154 (= S109), D174 (= D129), T175 (= T130), G176 (= G131), S178 (= S133), F206 (≠ L161), Y309 (≠ V240), Y310 (≠ D241), R358 (= R277), D425 (= D340)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 93% coverage: 20:386/394 of query aligns to 67:472/485 of 2dqnA
- active site: K79 (= K32), S154 (= S109), S155 (= S110), S173 (≠ T128), T175 (= T130), G176 (= G131), G177 (= G132), S178 (= S133), Q181 (≠ T136)
- binding asparagine: M129 (≠ Y84), G130 (≠ S85), T175 (= T130), G176 (= G131), S178 (= S133), Y309 (≠ V240), Y310 (≠ D241), R358 (= R277), D425 (= D340)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 93% coverage: 23:390/394 of query aligns to 82:464/605 of Q936X2
- K91 (= K32) mutation to A: Loss of activity.
- S165 (= S109) mutation to A: Loss of activity.
- S189 (= S133) mutation to A: Loss of activity.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 93% coverage: 23:388/394 of query aligns to 63:467/478 of 3h0mA
- active site: K72 (= K32), S147 (= S109), S148 (= S110), S166 (≠ T128), T168 (= T130), G169 (= G131), G170 (= G132), S171 (= S133), Q174 (≠ T136)
- binding glutamine: M122 (≠ Y84), G123 (≠ S85), D167 (= D129), T168 (= T130), G169 (= G131), G170 (= G132), S171 (= S133), F199 (≠ L161), Y302 (≠ G252), R351 (= R296), D418 (≠ H339)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 93% coverage: 23:388/394 of query aligns to 63:467/478 of 3h0lA
- active site: K72 (= K32), S147 (= S109), S148 (= S110), S166 (≠ T128), T168 (= T130), G169 (= G131), G170 (= G132), S171 (= S133), Q174 (≠ T136)
- binding asparagine: G123 (≠ S85), S147 (= S109), G169 (= G131), G170 (= G132), S171 (= S133), Y302 (≠ G252), R351 (= R296), D418 (≠ H339)
3kfuE Crystal structure of the transamidosome (see paper)
29% identity, 93% coverage: 23:388/394 of query aligns to 56:455/468 of 3kfuE
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 95% coverage: 2:376/394 of query aligns to 33:396/412 of 1o9oA
- active site: K62 (= K32), A131 (≠ S109), S132 (= S110), T150 (= T128), T152 (= T130), G153 (= G131), G154 (= G132), S155 (= S133), R158 (≠ T136)
- binding 3-amino-3-oxopropanoic acid: G130 (= G108), T152 (= T130), G153 (= G131), G154 (= G132), S155 (= S133), R158 (≠ T136), P359 (≠ L337)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 95% coverage: 2:376/394 of query aligns to 33:396/412 of 1ocmA
- active site: K62 (= K32), S131 (= S109), S132 (= S110), T152 (= T130), G153 (= G131), G154 (= G132), S155 (= S133)
- binding pyrophosphate 2-: R113 (vs. gap), S131 (= S109), Q151 (≠ D129), T152 (= T130), G153 (= G131), G154 (= G132), S155 (= S133), R158 (≠ T136), P359 (≠ L337)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
29% identity, 92% coverage: 21:384/394 of query aligns to 58:465/482 of 3a2qA
- active site: K69 (= K32), S147 (= S109), S148 (= S110), N166 (≠ T128), A168 (≠ T130), A169 (≠ G131), G170 (= G132), A171 (≠ S133), I174 (≠ T136)
- binding 6-aminohexanoic acid: G121 (≠ A83), G121 (≠ A83), N122 (≠ Y84), S147 (= S109), A168 (≠ T130), A168 (≠ T130), A169 (≠ G131), A171 (≠ S133), C313 (vs. gap)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
38% identity, 39% coverage: 22:174/394 of query aligns to 85:235/508 of 3a1iA
- active site: K95 (= K32), S170 (= S109), S171 (= S110), G189 (≠ T128), Q191 (≠ T130), G192 (= G131), G193 (= G132), A194 (≠ S133), I197 (≠ T136)
- binding benzamide: F145 (≠ Y84), S146 (= S85), G147 (≠ M86), Q191 (≠ T130), G192 (= G131), G193 (= G132), A194 (≠ S133)
Sites not aligning to the query:
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
33% identity, 47% coverage: 1:185/394 of query aligns to 12:192/450 of 4n0iA
- active site: K38 (= K32), S116 (= S109), S117 (= S110), T135 (= T128), T137 (= T130), G138 (= G131), G139 (= G132), S140 (= S133), L143 (≠ T136)
- binding glutamine: G89 (≠ S85), T137 (= T130), G138 (= G131), S140 (= S133), Y168 (≠ L161)
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
33% identity, 34% coverage: 20:153/394 of query aligns to 65:196/457 of 5h6sC
- active site: K77 (= K32), S152 (= S109), S153 (= S110), L173 (≠ T130), G174 (= G131), G175 (= G132), S176 (= S133)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A83), R128 (≠ S85), W129 (≠ M86), S152 (= S109), L173 (≠ T130), G174 (= G131), S176 (= S133)
Sites not aligning to the query:
Query Sequence
>BWI76_RS07545 FitnessBrowser__Koxy:BWI76_RS07545
MQDDLRAFMPYPPHPVAHALSGPLSGLTFAVKDLFDVAGYPTGGGNPHLLALSGIKNRTA
PVVQTLLNNGARFIGKTHTSELAYSMSGHNVHYGTPRNGAAPNHIPGGSSSGSASAVSNE
VCDFALGTDTGGSVRTPASYCGLFGLRPTHGRLSLDGCQPLCATMDTCGFFARSPEVFSA
VAACLFADERADLSGVRLACHDGLFSRLPLRSQQALQPVRQRLARFFGAVTPLAAPLPDV
DDIYLAFRQIQGYEAWQAQGETIERYGLQLGSDVRERFFWGKAVTRAQFDAACQQRVRFA
AWWDAQLGDAVLVMPTVPDGAPLLTAQAEEIEAVRRLSHDLLLISVMTQRPQVTLPVAQT
GGLPLGISFLGPRGSDRLLVELAAAFMQGDRNEQ
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