SitesBLAST
Comparing GFF3276 FitnessBrowser__Phaeo:GFF3276 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, 88% coverage: 50:439/442 of query aligns to 175:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A129), T258 (≠ G132), S281 (= S155), G302 (≠ T176), G303 (= G177), S305 (= S179), S472 (≠ R327), I532 (≠ Y384), M539 (= M391)
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, 88% coverage: 50:439/442 of query aligns to 175:589/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 155:156) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 176:179) binding substrate
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ N234) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
30% identity, 88% coverage: 50:439/442 of query aligns to 175:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A129), G302 (≠ T176), G303 (= G177), G304 (= G178), A305 (≠ S179), V442 (≠ A298), I475 (≠ S330), M539 (= M391)
Sites not aligning to the query:
8ey1D Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with n-(3-oxododecanoyl)-l-homoserine lactone
30% identity, 88% coverage: 50:439/442 of query aligns to 175:589/605 of 8ey1D
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 97% coverage: 10:439/442 of query aligns to 9:477/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (= S156), T179 (≠ S174), T181 (= T176), D182 (≠ G177), G183 (= G178), S184 (= S179), C187 (≠ I182)
- binding : A129 (= A129), N130 (vs. gap), F131 (vs. gap), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ I182), I212 (≠ L207), R318 (vs. gap), L321 (≠ V289), L365 (≠ I324), F426 (≠ Y385)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 98% coverage: 7:438/442 of query aligns to 6:473/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (= S174), T175 (= T176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ I182)
- binding glutamine: G130 (≠ S131), S154 (= S155), D174 (= D175), T175 (= T176), G176 (= G177), S178 (= S179), F206 (≠ L207), Y309 (≠ S297), Y310 (≠ A298), R358 (vs. gap), D425 (≠ A392)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 98% coverage: 7:438/442 of query aligns to 6:473/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (= S174), T175 (= T176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ I182)
- binding asparagine: M129 (≠ F130), G130 (≠ S131), T175 (= T176), G176 (= G177), S178 (= S179), Y309 (≠ S297), Y310 (≠ A298), R358 (vs. gap), D425 (≠ A392)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 98% coverage: 7:441/442 of query aligns to 5:469/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (= S174), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ I182)
- binding glutamine: M122 (≠ F130), G123 (≠ S131), D167 (= D175), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), F199 (≠ L207), Y302 (≠ S297), R351 (= R327), D418 (≠ S388)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 98% coverage: 7:441/442 of query aligns to 5:469/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (= S174), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ I182)
- binding asparagine: G123 (≠ S131), S147 (= S155), G169 (= G177), G170 (= G178), S171 (= S179), Y302 (≠ S297), R351 (= R327), D418 (≠ S388)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 84% coverage: 72:441/442 of query aligns to 92:490/507 of Q84DC4
- K100 (= K80) mutation to A: Abolishes activity on mandelamide.
- S180 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G177) 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 (= S179) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I182) 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 (≠ A293) 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 (≠ L355) 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 (≠ L393) 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.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 84% coverage: 49:418/442 of query aligns to 44:414/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (= S156), T165 (≠ S174), T167 (= T176), A168 (≠ G177), G169 (= G178), S170 (= S179), V173 (≠ I182)
- binding malonate ion: A120 (= A129), G122 (≠ S131), S146 (= S155), T167 (= T176), A168 (≠ G177), S170 (= S179), S193 (≠ E202), G194 (= G203), V195 (= V204), R200 (≠ L209), Y297 (≠ S297), R305 (≠ A305)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 83% coverage: 71:439/442 of query aligns to 86:498/508 of 3a1iA
- active site: K95 (= K80), S170 (= S155), S171 (= S156), G189 (≠ S174), Q191 (≠ T176), G192 (= G177), G193 (= G178), A194 (≠ S179), I197 (= I182)
- binding benzamide: F145 (= F130), S146 (= S131), G147 (= G132), Q191 (≠ T176), G192 (= G177), G193 (= G178), A194 (≠ S179), W327 (≠ S297)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 89% coverage: 50:442/442 of query aligns to 62:466/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (= S155) mutation to A: Loss of activity.
- S189 (= S179) mutation to A: Loss of activity.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 89% coverage: 44:438/442 of query aligns to 38:448/457 of 6c6gA
Q9AHE8 Urethanase; Enantioselective amidase; Ethyl carbamate-degrading amidase; EC 3.5.1.75 from Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter) (see 3 papers)
25% identity, 81% coverage: 55:413/442 of query aligns to 81:481/517 of Q9AHE8
- R94 (= R68) mutation to P: No change in activity.
- I97 (≠ L71) mutation to L: 1.12-fold increase in specific activity toward ethyl carbamate, shows higher ethanol tolerance. 3.1-fold increase in specific activity toward ethyl carbamate and 1.5-fold increase in ethanol tolerance, shows lower pH tolerance; when associated with A-195.
- K98 (= K80) mutation to A: Almost loss of activity.
- P163 (≠ I145) mutation to A: Decrease in activity.
- A172 (≠ G154) mutation to G: Changes substrate specificity. Decrease in activity.
- S173 (= S155) mutation to A: Almost loss of activity.
- N175 (≠ S157) mutation to G: Decrease in activity.; mutation to S: Changes substrate specificity.
- G195 (= G177) mutation to A: 1.86-fold increase in specific activity toward ethyl carbamate, shows lower pH tolerance, causes a decrease in the thermostability. 3.1-fold increase in specific activity toward ethyl carbamate and 1.5-fold increase in ethanol tolerance, shows lower pH tolerance; when associated with L-97.
- S197 (= S179) mutation to A: Almost loss of activity.
- L200 (≠ I182) mutation to C: Decrease in activity.
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 96% coverage: 19:442/442 of query aligns to 12:458/468 of 3kfuE
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
36% identity, 55% coverage: 10:253/442 of query aligns to 8:248/564 of 6te4A
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 91% coverage: 37:439/442 of query aligns to 26:445/457 of 5h6sC
- active site: K77 (= K80), S152 (= S155), S153 (= S156), L173 (≠ T176), G174 (= G177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A129), R128 (≠ S131), W129 (≠ G132), S152 (= S155), L173 (≠ T176), G174 (= G177), S176 (= S179), W306 (≠ S297), F338 (= F328)
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)
41% identity, 33% coverage: 72:219/442 of query aligns to 28:177/425 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 (= S155) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S156) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D175) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S179) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N187) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
24% identity, 80% coverage: 70:423/442 of query aligns to 28:435/450 of 4n0iA
- active site: K38 (= K80), S116 (= S155), S117 (= S156), T135 (≠ S174), T137 (= T176), G138 (= G177), G139 (= G178), S140 (= S179), L143 (≠ I182)
- binding glutamine: G89 (≠ S131), T137 (= T176), G138 (= G177), S140 (= S179), Y168 (≠ L207), Y271 (≠ S297), Y272 (≠ A298), R320 (vs. gap), D404 (≠ L393)
Query Sequence
>GFF3276 FitnessBrowser__Phaeo:GFF3276
MQEWLTQTAANLGRGIDAGDICPVALTKTYLNAIDAHPHRDRIYTVVTHDRALAEAEAAR
QRAADGQRLSLLDGVPISWKDLFDSATIATESGSDLLANRIPDRDALVLRSATAMGAVCL
GKTHMSELAFSGLGLNPVKATPPCIHDDAAAPGGSSSGAATSVAFGLAACGIGSDTGGSV
RIPAAWNGLVGLKTTSGRISLEGVVPLCLRFDTVGPLARSVEDAALYLGVLEGNHGPDLR
GASLAGKRFADLWTVAQQDLAPEVANAHSKALDRLRAAGAEIIPLEVPVLEEAMALSAVL
FTSEAYGLWKDVIEAAPDLMFPEILERFRSGAGFSGPDYVAAWAKLEQFRMDWDLATAGF
DGILCPTSPILPPNVARLQSDHDYYIHSNLMALRNTRIGNLMGLCALTLPTGVPSCGLQI
LGQPDCEEALLRIGAAVERALA
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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