SitesBLAST
Comparing Pf6N2E2_1873 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1873 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)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
31% identity, 97% coverage: 10:470/476 of query aligns to 5:479/490 of 4yjiA
- active site: K79 (= K84), S158 (= S159), S159 (= S160), G179 (= G180), G180 (= G181), G181 (= G182), A182 (≠ S183)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ G86), G132 (= G133), S158 (= S159), G179 (= G180), G180 (= G181), A182 (≠ S183)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 96% coverage: 6:463/476 of query aligns to 1:473/485 of 2f2aA
- active site: K79 (= K84), S154 (= S159), S155 (= S160), S173 (≠ T178), T175 (≠ G180), G176 (= G181), G177 (= G182), S178 (= S183), Q181 (≠ V186)
- binding glutamine: G130 (≠ S135), S154 (= S159), D174 (= D179), T175 (≠ G180), G176 (= G181), S178 (= S183), F206 (≠ P210), Y309 (≠ A311), Y310 (≠ W312), R358 (vs. gap), D425 (≠ W412)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 96% coverage: 6:463/476 of query aligns to 1:473/485 of 2dqnA
- active site: K79 (= K84), S154 (= S159), S155 (= S160), S173 (≠ T178), T175 (≠ G180), G176 (= G181), G177 (= G182), S178 (= S183), Q181 (≠ V186)
- binding asparagine: M129 (≠ H134), G130 (≠ S135), T175 (≠ G180), G176 (= G181), S178 (= S183), Y309 (≠ A311), Y310 (≠ W312), R358 (vs. gap), D425 (≠ W412)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 95% coverage: 11:463/476 of query aligns to 5:444/457 of 5h6sC
- active site: K77 (= K84), S152 (= S159), S153 (= S160), L173 (≠ G180), G174 (= G181), G175 (= G182), S176 (= S183)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G133), R128 (≠ S135), W129 (≠ A136), S152 (= S159), L173 (≠ G180), G174 (= G181), S176 (= S183), W306 (= W321), F338 (vs. gap)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 82% coverage: 76:463/476 of query aligns to 87:497/508 of 3a1iA
- active site: K95 (= K84), S170 (= S159), S171 (= S160), G189 (≠ T178), Q191 (≠ G180), G192 (= G181), G193 (= G182), A194 (≠ S183), I197 (≠ V186)
- binding benzamide: F145 (≠ H134), S146 (= S135), G147 (≠ A136), Q191 (≠ G180), G192 (= G181), G193 (= G182), A194 (≠ S183), W327 (= W312)
3kfuE Crystal structure of the transamidosome (see paper)
30% identity, 97% coverage: 13:475/476 of query aligns to 2:466/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 93% coverage: 20:463/476 of query aligns to 14:466/478 of 3h0mA
- active site: K72 (= K84), S147 (= S159), S148 (= S160), S166 (≠ T178), T168 (≠ G180), G169 (= G181), G170 (= G182), S171 (= S183), Q174 (≠ V186)
- binding glutamine: M122 (≠ H134), G123 (≠ S135), D167 (= D179), T168 (≠ G180), G169 (= G181), G170 (= G182), S171 (= S183), F199 (≠ P210), Y302 (≠ A311), R351 (≠ L342), D418 (≠ W412)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 93% coverage: 20:463/476 of query aligns to 14:466/478 of 3h0lA
- active site: K72 (= K84), S147 (= S159), S148 (= S160), S166 (≠ T178), T168 (≠ G180), G169 (= G181), G170 (= G182), S171 (= S183), Q174 (≠ V186)
- binding asparagine: G123 (≠ S135), S147 (= S159), G169 (= G181), G170 (= G182), S171 (= S183), Y302 (≠ A311), R351 (≠ L342), D418 (≠ W412)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
29% identity, 99% coverage: 4:474/476 of query aligns to 4:484/487 of 1m21A
- active site: K81 (= K84), S160 (= S159), S161 (= S160), T179 (= T178), T181 (≠ G180), D182 (≠ G181), G183 (= G182), S184 (= S183), C187 (≠ V186)
- binding : A129 (vs. gap), N130 (vs. gap), F131 (vs. gap), C158 (≠ G157), G159 (= G158), S160 (= S159), S184 (= S183), C187 (≠ V186), I212 (vs. gap), R318 (≠ Q317), L321 (= L327), L365 (= L377), F426 (vs. gap)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
38% identity, 49% coverage: 8:242/476 of query aligns to 25:264/507 of Q84DC4
- T31 (= T14) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K84) mutation to A: Abolishes activity on mandelamide.
- S180 (= S159) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S160) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G181) 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 (= S183) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V186) 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.
Sites not aligning to the query:
- 316 S→N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- 382 Q→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.
- 437 I→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.
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
26% identity, 93% coverage: 20:463/476 of query aligns to 138:588/607 of Q7XJJ7
- K205 (= K84) mutation to A: Loss of activity.
- SS 281:282 (= SS 159:160) mutation to AA: Loss of activity.
- GGGS 302:305 (= GGGS 180:183) binding
- S305 (= S183) mutation to A: Loss of activity.
- R307 (= R185) mutation to A: Loss of activity.
- S360 (≠ Q237) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 93% coverage: 20:463/476 of query aligns to 138:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G133), T258 (≠ A136), S281 (= S159), G302 (= G180), G303 (= G181), S305 (= S183), S472 (= S347), I532 (vs. gap), M539 (≠ V410)
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 95% coverage: 11:463/476 of query aligns to 1:448/457 of 6c6gA
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
34% identity, 49% coverage: 13:246/476 of query aligns to 7:238/482 of 3a2qA
- active site: K69 (= K84), S147 (= S159), S148 (= S160), N166 (≠ T178), A168 (≠ G180), A169 (≠ G181), G170 (= G182), A171 (≠ S183), I174 (≠ V186)
- binding 6-aminohexanoic acid: G121 (= G133), G121 (= G133), N122 (≠ H134), S147 (= S159), A168 (≠ G180), A168 (≠ G180), A169 (≠ G181), A171 (≠ S183)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 92% coverage: 15:452/476 of query aligns to 6:427/461 of 4gysB
- active site: K72 (= K84), S146 (= S159), S147 (= S160), T165 (= T178), T167 (≠ G180), A168 (≠ G181), G169 (= G182), S170 (= S183), V173 (= V186)
- binding malonate ion: A120 (≠ G133), G122 (≠ S135), S146 (= S159), T167 (≠ G180), A168 (≠ G181), S170 (= S183), S193 (≠ D206), G194 (≠ T207), V195 (≠ L208), R200 (≠ E212), Y297 (≠ W312), R305 (≠ L320)
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)
32% identity, 41% coverage: 76:272/476 of query aligns to 28:246/425 of Q9FR37
- K36 (= K84) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S159) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S160) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D179) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S183) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ G191) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (= S244) mutation to T: Slightly reduces catalytic activity.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
27% identity, 91% coverage: 29:462/476 of query aligns to 37:460/605 of Q936X2
- K91 (= K84) mutation to A: Loss of activity.
- S165 (= S159) mutation to A: Loss of activity.
- S189 (= S183) 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)
32% identity, 48% coverage: 28:256/476 of query aligns to 22:261/564 of 6te4A
Sites not aligning to the query:
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)
31% identity, 46% coverage: 8:224/476 of query aligns to 74:287/579 of Q9TUI8
- S217 (= S159) mutation to A: Loss of activity.
- S218 (= S160) mutation to A: Lowers activity by at least 98%.
- D237 (= D179) mutation D->E,N: Loss of activity.
- S241 (= S183) mutation to A: Loss of activity.
- C249 (≠ G191) mutation to A: Loss of activity.
2wj1A 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with 7-phenyl-1-(4-(pyridin-2-yl)oxazol-2-yl) heptan- 1-one, an alpha-ketooxazole (see paper)
31% identity, 54% coverage: 17:273/476 of query aligns to 50:298/543 of 2wj1A
- active site: K109 (= K84), S184 (= S159), S185 (= S160), T203 (= T178), I205 (≠ G180), G206 (= G181), G207 (= G182), S208 (= S183), F211 (≠ V186)
- binding 7-phenyl-1-(4-pyridin-2-yl-1,3-oxazol-2-yl)heptane-1,1-diol: S157 (≠ F132), M158 (≠ G133), F159 (≠ H134), S184 (= S159), T203 (= T178), D204 (= D179), I205 (≠ G180), G206 (= G181), S208 (= S183), C236 (vs. gap)
Sites not aligning to the query:
Query Sequence
>Pf6N2E2_1873 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1873
MSKSELDLCYLTATEAVAQFKAKTLSPVDVLRAQIARIEAVNSKLNAITYTHFDRALKEA
QVAEGLYMRGVATRPLEGVTCAIKDGNPIKGEIMTVGSKAFADFIPDESAPTVERLIDAG
AIVHCRTTMSEFGHSAITKSPLWGVTRNAWNPEYSSGGSSGGAGSALAAGMTTLADGTDG
GGSIRVPAALGGLFGYKPPFGRNPVDTLSPGETLMHYGPLARSVADCALMQNVMSGQHPK
DLYSLPDQVVLPTFGESLRGRRIALSMNLGFYEVSKEVRENTLAAAEVFRGLGCIVEEIQ
LPWERASVEDAWLIKWQALLWAQCGDLLPEFRNDLDPFVVELMEQGSHLDLRRFYRTNQT
KHEMHQALVAAMSGYDLLIAPTTATTQIPADRHDADPLLINGKAIDRPYVGWLLTTPFNL
LSQYPVFSVPSGVDQTTSIPTGLQIIGPAYDDLAVFSAAYTFEAATQPWSFRRPLL
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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