SitesBLAST
Comparing HSERO_RS09160 FitnessBrowser__HerbieS:HSERO_RS09160 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)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
34% identity, 82% coverage: 12:379/450 of query aligns to 10:379/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 99% coverage: 4:448/450 of query aligns to 29:490/507 of Q84DC4
- T31 (≠ S6) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K77) mutation to A: Abolishes activity on mandelamide.
- S180 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S158) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G179) 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 (= S181) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I184) 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 (≠ L295) 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 (≠ A340) 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 (≠ L397) 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.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 91% coverage: 39:446/450 of query aligns to 41:474/485 of 2f2aA
- active site: K79 (= K77), S154 (= S157), S155 (= S158), S173 (= S176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ I184)
- binding glutamine: G130 (≠ S129), S154 (= S157), D174 (= D177), T175 (= T178), G176 (= G179), S178 (= S181), F206 (≠ L209), Y309 (≠ F292), Y310 (≠ N293), R358 (= R331), D425 (≠ K395)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 91% coverage: 39:446/450 of query aligns to 41:474/485 of 2dqnA
- active site: K79 (= K77), S154 (= S157), S155 (= S158), S173 (= S176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ I184)
- binding asparagine: M129 (≠ Y128), G130 (≠ S129), T175 (= T178), G176 (= G179), S178 (= S181), Y309 (≠ F292), Y310 (≠ N293), R358 (= R331), D425 (≠ K395)
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)
29% identity, 83% coverage: 69:440/450 of query aligns to 28:417/425 of Q9FR37
- K36 (= K77) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S157) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S158) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D177) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S181) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N189) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (vs. gap) mutation to T: Slightly reduces catalytic activity.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 85% coverage: 67:447/450 of query aligns to 195:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A127), T258 (≠ G130), S281 (= S157), G302 (≠ T178), G303 (= G179), S305 (= S181), S472 (≠ V329), I532 (≠ Y390), M539 (≠ L397)
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, 85% coverage: 67:447/450 of query aligns to 195:590/607 of Q7XJJ7
- K205 (= K77) mutation to A: Loss of activity.
- SS 281:282 (= SS 157:158) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 178:181) binding
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (≠ E236) mutation to A: No effect.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 91% coverage: 4:414/450 of query aligns to 4:406/461 of 4gysB
- active site: K72 (= K77), S146 (= S157), S147 (= S158), T165 (≠ S176), T167 (= T178), A168 (≠ G179), G169 (= G180), S170 (= S181), V173 (≠ I184)
- binding malonate ion: A120 (= A127), G122 (≠ S129), S146 (= S157), T167 (= T178), A168 (≠ G179), S170 (= S181), S193 (≠ Q204), G194 (= G205), V195 (= V206), R200 (≠ A211), Y297 (≠ A300), R305 (vs. gap)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 98% coverage: 3:445/450 of query aligns to 5:466/478 of 3h0mA
- active site: K72 (= K77), S147 (= S157), S148 (= S158), S166 (= S176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ I184)
- binding glutamine: M122 (≠ Y128), G123 (≠ S129), D167 (= D177), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (≠ L209), Y302 (≠ F292), R351 (= R331), D418 (≠ N393)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 98% coverage: 3:445/450 of query aligns to 5:466/478 of 3h0lA
- active site: K72 (= K77), S147 (= S157), S148 (= S158), S166 (= S176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ I184)
- binding asparagine: G123 (≠ S129), S147 (= S157), G169 (= G179), G170 (= G180), S171 (= S181), Y302 (≠ F292), R351 (= R331), D418 (≠ N393)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 97% coverage: 8:445/450 of query aligns to 11:476/487 of 1m21A
- active site: K81 (= K77), S160 (= S157), S161 (= S158), T179 (≠ S176), T181 (= T178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (≠ I184)
- binding : A129 (= A127), N130 (≠ Y128), F131 (vs. gap), C158 (≠ G155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (≠ I184), I212 (≠ L209), R318 (≠ N293), L321 (≠ A296), L365 (≠ M338), F426 (≠ Y389)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 85% coverage: 69:450/450 of query aligns to 87:502/508 of 3a1iA
- active site: K95 (= K77), S170 (= S157), S171 (= S158), G189 (≠ S176), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), I197 (= I184)
- binding benzamide: F145 (≠ Y128), S146 (= S129), G147 (= G130), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), W327 (≠ L295)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 85% coverage: 68:449/450 of query aligns to 82:466/605 of Q936X2
- K91 (= K77) mutation to A: Loss of activity.
- S165 (= S157) mutation to A: Loss of activity.
- S189 (= S181) mutation to A: Loss of activity.
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 84% coverage: 68:445/450 of query aligns to 56:454/468 of 3kfuE
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
32% identity, 52% coverage: 4:236/450 of query aligns to 6:240/564 of 6te4A
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 64% coverage: 4:293/450 of query aligns to 6:300/457 of 5h6sC
- active site: K77 (= K77), S152 (= S157), S153 (= S158), L173 (≠ T178), G174 (= G179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A127), R128 (≠ S129), W129 (≠ G130), S152 (= S157), L173 (≠ T178), G174 (= G179), S176 (= S181)
Sites not aligning to the query:
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
40% identity, 32% coverage: 76:220/450 of query aligns to 68:209/593 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.
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
32% identity, 43% coverage: 45:237/450 of query aligns to 100:301/579 of Q9TUI8
- S217 (≠ G156) mutation to A: Loss of activity.
- S218 (= S157) mutation to A: Lowers activity by at least 98%.
- D237 (= D177) mutation D->E,N: Loss of activity.
- S241 (= S181) mutation to A: Loss of activity.
- C249 (≠ N189) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 85% coverage: 68:449/450 of query aligns to 53:411/412 of 1o9oA
- active site: K62 (= K77), A131 (≠ S157), S132 (= S158), T150 (≠ S176), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ I184)
- binding 3-amino-3-oxopropanoic acid: G130 (= G156), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ I184), P359 (≠ A388)
2wapA 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with the drug-like urea inhibitor pf-3845 (see paper)
35% identity, 35% coverage: 69:224/450 of query aligns to 102:256/541 of 2wapA
- active site: K110 (= K77), S185 (= S157), S186 (= S158), T204 (≠ S176), I206 (≠ T178), G207 (= G179), G208 (= G180), S209 (= S181), F212 (≠ I184)
- binding 4-(3-{[5-(trifluoromethyl)pyridin-2-yl]oxy}benzyl)piperidine-1-carboxylic acid: F160 (≠ Y128), S161 (= S129), I206 (≠ T178), G207 (= G179), S209 (= S181)
Sites not aligning to the query:
Query Sequence
>HSERO_RS09160 FitnessBrowser__HerbieS:HSERO_RS09160
MPSTLSRLAADLAAGHTTSLQLTEQALARIADPAGEGARVFTRVYAEQARAAARASDTLR
AARLCRSPLEGVPVSVKDLFDVAGETTLAGSVVLRGKPVASAHAAVVQNLLKAGAILIGK
TNMTEFAYSGLGINPHYGTPQNAWERNIEGGRIPGGSSSGAAISVTDGMAFAAVGSDTGG
SVRIPSALNGLTGFKPTAARVSMQGVLPLSAYLDSIGPLAVSVQCCAIMDAVLAGEDYVA
VLAHPLRGLRLLAPTNVVLDGMDDTVGQAYRTALGKLAAAGAMIVEAEVPAFNALAAINA
KGGFTAAEAYAWHRALIAENAAGYDQRVVSRILRGKDMSAADLLDVLHARPRWIAQVEAQ
LAGYDALVMPTVPIVAPRIAELQASDDAYYGANGKMLRNPTLINFLDGCALSLPCHAPGS
APVGLSLAACGGQDKRLLSIGLAVEALLAA
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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