SitesBLAST
Comparing Pf6N2E2_3707 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_3707 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)
42% identity, 50% coverage: 14:240/457 of query aligns to 4:231/457 of 6c6gA
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
31% identity, 94% coverage: 25:452/457 of query aligns to 23:474/485 of 2f2aA
- active site: K79 (= K81), S154 (= S159), S155 (= S160), S173 (≠ T178), T175 (= T180), G176 (≠ A181), G177 (= G182), S178 (= S183), Q181 (≠ V186)
- binding glutamine: G130 (≠ S133), S154 (= S159), D174 (= D179), T175 (= T180), G176 (≠ A181), S178 (= S183), F206 (≠ L211), Y309 (vs. gap), Y310 (vs. gap), R358 (= R337), D425 (≠ L402)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
31% identity, 94% coverage: 25:452/457 of query aligns to 23:474/485 of 2dqnA
- active site: K79 (= K81), S154 (= S159), S155 (= S160), S173 (≠ T178), T175 (= T180), G176 (≠ A181), G177 (= G182), S178 (= S183), Q181 (≠ V186)
- binding asparagine: M129 (≠ Y132), G130 (≠ S133), T175 (= T180), G176 (≠ A181), S178 (= S183), Y309 (vs. gap), Y310 (vs. gap), R358 (= R337), D425 (≠ L402)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 98% coverage: 4:451/457 of query aligns to 122:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A131), T258 (≠ G134), S281 (= S159), G302 (≠ T180), G303 (≠ A181), S305 (= S183), S472 (≠ R337), I532 (≠ L393), M539 (≠ L402)
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)
26% identity, 98% coverage: 4:451/457 of query aligns to 122:588/607 of Q7XJJ7
- K205 (= K81) mutation to A: Loss of activity.
- SS 281:282 (= SS 159:160) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 180:183) binding
- S305 (= S183) mutation to A: Loss of activity.
- R307 (= R185) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 90% coverage: 43:455/457 of query aligns to 62:491/507 of Q84DC4
- K100 (= K81) 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 (≠ A181) 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.
- S316 (≠ R291) 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 (≠ A346) 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 (≠ L402) 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.
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, 83% coverage: 75:454/457 of query aligns to 30:425/425 of Q9FR37
- K36 (= K81) 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 (≠ N191) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ A259) mutation to T: Slightly reduces catalytic activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
34% identity, 92% coverage: 29:447/457 of query aligns to 20:434/461 of 4gysB
- active site: K72 (= K81), S146 (= S159), S147 (= S160), T165 (= T178), T167 (= T180), A168 (= A181), G169 (= G182), S170 (= S183), V173 (= V186)
- binding malonate ion: A120 (= A131), G122 (≠ S133), S146 (= S159), T167 (= T180), A168 (= A181), S170 (= S183), S193 (≠ D206), G194 (= G207), V195 (= V208), R200 (≠ H213), Y297 (≠ R304), R305 (≠ E313)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 75% coverage: 107:451/457 of query aligns to 120:497/508 of 3a1iA
- active site: S170 (= S159), S171 (= S160), G189 (≠ T178), Q191 (≠ T180), G192 (≠ A181), G193 (= G182), A194 (≠ S183), I197 (≠ V186)
- binding benzamide: F145 (≠ Y132), S146 (= S133), G147 (= G134), Q191 (≠ T180), G192 (≠ A181), G193 (= G182), A194 (≠ S183), W327 (≠ S299)
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 96% coverage: 21:457/457 of query aligns to 10:460/468 of 3kfuE
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
42% identity, 37% coverage: 73:239/457 of query aligns to 73:240/487 of 1m21A
- active site: K81 (= K81), S160 (= S159), S161 (= S160), T179 (= T178), T181 (= T180), D182 (≠ A181), G183 (= G182), S184 (= S183), C187 (≠ V186)
- binding : A129 (= A131), N130 (≠ Y132), F131 (vs. gap), C158 (≠ G157), G159 (= G158), S160 (= S159), S184 (= S183), C187 (≠ V186), I212 (≠ L211)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
32% identity, 86% coverage: 63:456/457 of query aligns to 74:467/605 of Q936X2
- K91 (= K81) mutation to A: Loss of activity.
- S165 (= S159) mutation to A: Loss of activity.
- S189 (= S183) mutation to A: Loss of activity.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 96% coverage: 16:456/457 of query aligns to 10:471/478 of 3h0mA
- active site: K72 (= K81), S147 (= S159), S148 (= S160), S166 (≠ T178), T168 (= T180), G169 (≠ A181), G170 (= G182), S171 (= S183), Q174 (≠ V186)
- binding glutamine: M122 (≠ Y132), G123 (≠ S133), D167 (= D179), T168 (= T180), G169 (≠ A181), G170 (= G182), S171 (= S183), F199 (≠ L211), Y302 (vs. gap), R351 (= R337), D418 (≠ T401)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 96% coverage: 16:456/457 of query aligns to 10:471/478 of 3h0lA
- active site: K72 (= K81), S147 (= S159), S148 (= S160), S166 (≠ T178), T168 (= T180), G169 (≠ A181), G170 (= G182), S171 (= S183), Q174 (≠ V186)
- binding asparagine: G123 (≠ S133), S147 (= S159), G169 (≠ A181), G170 (= G182), S171 (= S183), Y302 (vs. gap), R351 (= R337), D418 (≠ T401)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 86% coverage: 29:421/457 of query aligns to 23:423/457 of 5h6sC
- active site: K77 (= K81), S152 (= S159), S153 (= S160), L173 (≠ T180), G174 (≠ A181), G175 (= G182), S176 (= S183)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A131), R128 (≠ S133), W129 (≠ G134), S152 (= S159), L173 (≠ T180), G174 (≠ A181), S176 (= S183), W306 (= W308), F338 (≠ E339)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
26% identity, 84% coverage: 69:450/457 of query aligns to 26:449/450 of 4n0iA
- active site: K38 (= K81), S116 (= S159), S117 (= S160), T135 (= T178), T137 (= T180), G138 (≠ A181), G139 (= G182), S140 (= S183), L143 (≠ V186)
- binding glutamine: G89 (≠ S133), T137 (= T180), G138 (≠ A181), S140 (= S183), Y168 (≠ L211), Y271 (≠ H306), Y272 (≠ G307), R320 (= R337), D404 (≠ L402)
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
42% identity, 36% coverage: 78:242/457 of query aligns to 66:235/593 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.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
33% identity, 51% coverage: 13:247/457 of query aligns to 8:248/490 of 4yjiA
- active site: K79 (= K81), S158 (= S159), S159 (= S160), G179 (≠ T180), G180 (≠ A181), G181 (= G182), A182 (≠ S183)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L83), G132 (≠ A131), S158 (= S159), G179 (≠ T180), G180 (≠ A181), A182 (≠ S183)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
32% identity, 49% coverage: 16:240/457 of query aligns to 10:241/564 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)
32% identity, 46% coverage: 16:226/457 of query aligns to 82:288/579 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 (≠ N191) mutation to A: Loss of activity.
Query Sequence
>Pf6N2E2_3707 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_3707
MPLPMNAFSSPDAIALAEAFASGRTDPVQVLEQALEQASRAEHVFVSLTEARARREAQAS
AARWRAGQPLSGFDGVPLAWKDLFDVAGSVTTAAAAVRRDAPPALLDAASVSLLSRAGMV
CLGKTNLSEFAYSGLGLNPHFGTPVNPFSDAQPRIPGGSSSGSAVAVAAGIVPIAMGTDT
AGSIRVPAAFNALVGFRASSRRHSRDGVFPLAHSIDSIGPLTRSVRDAWMIDELLQGRDP
RQAPPVRSLAGQRFWVEQAVLEDASVEAAVRANVLAGVQALRTAGALVEIRPLPAFQASL
ALIRDHGWLGAAEAFALHEALLDSADAERLDPRVRRRLEAARPMTASQVLKLYDARSALQ
RQLVEELDGAVLITPTVAHVAPPLAPLEADDELFVRTNLATLRLTMPGSLLDMPSVNLPS
GRDSQGLPTGLLLSVPQGEDARLLRVARSVEATLANS
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