SitesBLAST
Comparing YP_001328648.1 NCBI__GCF_000017145.1:YP_001328648.1 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)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 90% coverage: 40:431/435 of query aligns to 180:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A115), T258 (≠ A118), S281 (= S141), G302 (≠ S162), G303 (= G163), S305 (= S165), S472 (≠ K314), I532 (≠ Y374), M539 (≠ L382)
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)
30% identity, 90% coverage: 40:431/435 of query aligns to 180:590/607 of Q7XJJ7
- K205 (= K65) mutation to A: Loss of activity.
- SS 281:282 (= SS 141:142) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ SGGS 162:165) binding
- S305 (= S165) mutation to A: Loss of activity.
- R307 (= R167) mutation to A: Loss of activity.
- S360 (≠ E220) mutation to A: No effect.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 96% coverage: 8:423/435 of query aligns to 17:442/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 98% coverage: 8:435/435 of query aligns to 44:493/507 of Q84DC4
- K100 (= K65) mutation to A: Abolishes activity on mandelamide.
- S180 (= S141) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S142) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G163) 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 (= S165) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I168) 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 (≠ A281) 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 (≠ R333) 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 (≠ L382) 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.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 87% coverage: 53:431/435 of query aligns to 83:499/508 of 3a1iA
- active site: K95 (= K65), S170 (= S141), S171 (= S142), G189 (≠ S160), Q191 (≠ S162), G192 (= G163), G193 (= G164), A194 (≠ S165), I197 (= I168)
- binding benzamide: F145 (= F116), S146 (≠ T117), G147 (≠ A118), Q191 (≠ S162), G192 (= G163), G193 (= G164), A194 (≠ S165), W327 (≠ A283)
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)
27% identity, 86% coverage: 57:432/435 of query aligns to 28:425/425 of Q9FR37
- K36 (= K65) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S141) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S142) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D161) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S165) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ Q173) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ G236) mutation to T: Slightly reduces catalytic activity.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
26% identity, 93% coverage: 27:429/435 of query aligns to 41:473/485 of 2f2aA
- active site: K79 (= K65), S154 (= S141), S155 (= S142), S173 (= S160), T175 (≠ S162), G176 (= G163), G177 (= G164), S178 (= S165), Q181 (≠ I168)
- binding glutamine: G130 (≠ T117), S154 (= S141), D174 (= D161), T175 (≠ S162), G176 (= G163), S178 (= S165), F206 (≠ L193), Y309 (vs. gap), Y310 (vs. gap), R358 (= R320), D425 (≠ Q390)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
26% identity, 93% coverage: 27:429/435 of query aligns to 41:473/485 of 2dqnA
- active site: K79 (= K65), S154 (= S141), S155 (= S142), S173 (= S160), T175 (≠ S162), G176 (= G163), G177 (= G164), S178 (= S165), Q181 (≠ I168)
- binding asparagine: M129 (≠ F116), G130 (≠ T117), T175 (≠ S162), G176 (= G163), S178 (= S165), Y309 (vs. gap), Y310 (vs. gap), R358 (= R320), D425 (≠ Q390)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 95% coverage: 21:434/435 of query aligns to 32:471/478 of 3h0mA
- active site: K72 (= K65), S147 (= S141), S148 (= S142), S166 (= S160), T168 (≠ S162), G169 (= G163), G170 (= G164), S171 (= S165), Q174 (≠ I168)
- binding glutamine: M122 (≠ F116), G123 (vs. gap), D167 (= D161), T168 (≠ S162), G169 (= G163), G170 (= G164), S171 (= S165), F199 (≠ L193), Y302 (≠ L277), R351 (= R320), D418 (= D379)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 95% coverage: 21:434/435 of query aligns to 32:471/478 of 3h0lA
- active site: K72 (= K65), S147 (= S141), S148 (= S142), S166 (= S160), T168 (≠ S162), G169 (= G163), G170 (= G164), S171 (= S165), Q174 (≠ I168)
- binding asparagine: G123 (vs. gap), S147 (= S141), G169 (= G163), G170 (= G164), S171 (= S165), Y302 (≠ L277), R351 (= R320), D418 (= D379)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 94% coverage: 25:435/435 of query aligns to 51:468/605 of Q936X2
- K91 (= K65) mutation to A: Loss of activity.
- S165 (= S141) mutation to A: Loss of activity.
- S189 (= S165) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 87% coverage: 57:435/435 of query aligns to 64:444/461 of 4gysB
- active site: K72 (= K65), S146 (= S141), S147 (= S142), T165 (≠ S160), T167 (≠ S162), A168 (≠ G163), G169 (= G164), S170 (= S165), V173 (≠ I168)
- binding malonate ion: A120 (= A115), G122 (≠ T117), S146 (= S141), T167 (≠ S162), A168 (≠ G163), S170 (= S165), S193 (≠ E188), G194 (= G189), V195 (≠ A190), R200 (≠ P195), Y297 (≠ I286), R305 (≠ G291)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
40% identity, 47% coverage: 16:219/435 of query aligns to 33:238/487 of 1m21A
- active site: K81 (= K65), S160 (= S141), S161 (= S142), T179 (≠ S160), T181 (≠ S162), D182 (≠ G163), G183 (= G164), S184 (= S165), C187 (≠ I168)
- binding : A129 (= A115), N130 (vs. gap), F131 (= F116), C158 (≠ G139), G159 (= G140), S160 (= S141), S184 (= S165), C187 (≠ I168), I212 (≠ L193)
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 87% coverage: 57:434/435 of query aligns to 57:459/468 of 3kfuE
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
33% identity, 47% coverage: 27:230/435 of query aligns to 40:247/457 of 5h6sC
- active site: K77 (= K65), S152 (= S141), S153 (= S142), L173 (≠ S162), G174 (= G163), G175 (= G164), S176 (= S165)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A115), R128 (≠ T117), W129 (≠ A118), S152 (= S141), L173 (≠ S162), G174 (= G163), S176 (= S165)
Sites not aligning to the query:
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
26% identity, 91% coverage: 37:434/435 of query aligns to 54:554/564 of 6te4A
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 96% coverage: 17:434/435 of query aligns to 27:412/412 of 1o9oA
- active site: K62 (= K65), A131 (≠ S141), S132 (= S142), T150 (≠ S160), T152 (≠ S162), G153 (= G163), G154 (= G164), S155 (= S165), R158 (≠ I168)
- binding 3-amino-3-oxopropanoic acid: G130 (= G140), T152 (≠ S162), G153 (= G163), G154 (= G164), S155 (= S165), R158 (≠ I168), P359 (≠ D370)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
35% identity, 35% coverage: 57:207/435 of query aligns to 30:182/450 of 4n0iA
- active site: K38 (= K65), S116 (≠ G140), S117 (= S141), T135 (≠ S160), T137 (≠ S162), G138 (= G163), G139 (= G164), S140 (= S165), L143 (≠ I168)
- binding glutamine: G89 (≠ T117), T137 (≠ S162), G138 (= G163), S140 (= S165), Y168 (≠ L193)
Sites not aligning to the query:
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 96% coverage: 17:434/435 of query aligns to 27:412/412 of 1ocmA
- active site: K62 (= K65), S131 (= S141), S132 (= S142), T152 (≠ S162), G153 (= G163), G154 (= G164), S155 (= S165)
- binding pyrophosphate 2-: R113 (vs. gap), S131 (= S141), Q151 (≠ D161), T152 (≠ S162), G153 (= G163), G154 (= G164), S155 (= S165), R158 (≠ I168), P359 (≠ D370)
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
24% identity, 86% coverage: 63:434/435 of query aligns to 67:456/593 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
>YP_001328648.1 NCBI__GCF_000017145.1:YP_001328648.1
MPRPDMPSRDRLEAILAGLDLRRHEERAFVKLYPETARAEADAADRRRREKRSLGLLDGR
IVSVKDLFDIAGEPTLAGSIIRRAAPSATADAAIVRRLRAAGAVIIGKTHMTEFAFTAVG
LNPHYPVPGNATDRSLIPGGSSSGAAVSAAEGTSEIAIGSDSGGSVRIPAALQGLVGFKP
TARRIPLEGAFPLSPSLDSIGPLARTVADCAAADAIMAGETPRPLEPVPLAGMKLGMPKG
ALLEGLATEIAAAFERSLQALSRAGAKLAECGIDDLLTRFAEATAIGSLAGLEASRVHAD
WLRDENAPVDIRLKFPLRRRLAIPDSAIHDLLRTRQGLMRAMDERLRPFDFILMPATPIP
AVSIASVEEDRAEYRRVEDLLLRNTQVANQFDLTAITLPMPGMSLPAGLMLMGRNGTDGA
LLRLAASVERLLQRG
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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