SitesBLAST
Comparing GFF3601 FitnessBrowser__Marino:GFF3601 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
31% identity, 79% coverage: 78:447/470 of query aligns to 28:415/425 of Q9FR37
- K36 (= K86) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S164) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S165) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D184) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S188) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C196) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (vs. gap) mutation to T: Slightly reduces catalytic activity.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 92% coverage: 22:454/470 of query aligns to 9:448/457 of 6c6gA
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 92% coverage: 23:454/470 of query aligns to 14:466/478 of 3h0mA
- active site: K72 (= K86), S147 (≠ G162), S148 (≠ G163), S166 (≠ T183), T168 (= T185), G169 (≠ S186), G170 (= G187), S171 (= S188), Q174 (≠ I191)
- binding glutamine: M122 (≠ F137), G123 (≠ S138), D167 (= D184), T168 (= T185), G169 (≠ S186), G170 (= G187), S171 (= S188), F199 (≠ L216), Y302 (≠ A300), R351 (= R340), D418 (≠ N401)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 92% coverage: 23:454/470 of query aligns to 14:466/478 of 3h0lA
- active site: K72 (= K86), S147 (≠ G162), S148 (≠ G163), S166 (≠ T183), T168 (= T185), G169 (≠ S186), G170 (= G187), S171 (= S188), Q174 (≠ I191)
- binding asparagine: G123 (≠ S138), S147 (≠ G162), G169 (≠ S186), G170 (= G187), S171 (= S188), Y302 (≠ A300), R351 (= R340), D418 (≠ N401)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 80% coverage: 59:436/470 of query aligns to 178:570/607 of Q7XJJ7
- K205 (= K86) mutation to A: Loss of activity.
- SS 281:282 (= SS 164:165) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TSGS 185:188) binding
- S305 (= S188) mutation to A: Loss of activity.
- R307 (= R190) mutation to A: Loss of activity.
- S360 (≠ L243) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 80% coverage: 59:436/470 of query aligns to 178:570/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A136), T258 (≠ G139), S281 (= S164), G302 (≠ T185), G303 (≠ S186), S305 (= S188), S472 (≠ R340), I532 (≠ K398), M539 (≠ L405)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 81% coverage: 78:459/470 of query aligns to 92:492/507 of Q84DC4
- K100 (= K86) mutation to A: Abolishes activity on mandelamide.
- S180 (= S164) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S165) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ S186) 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 (= S188) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I191) 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 (≠ D303) 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 (≠ K350) 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 (= I404) 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.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 91% coverage: 38:464/470 of query aligns to 45:472/605 of Q936X2
- K91 (= K86) mutation to A: Loss of activity.
- S165 (= S164) mutation to A: Loss of activity.
- S189 (= S188) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 78% coverage: 78:444/470 of query aligns to 64:428/461 of 4gysB
- active site: K72 (= K86), S146 (= S164), S147 (= S165), T165 (= T183), T167 (= T185), A168 (≠ S186), G169 (= G187), S170 (= S188), V173 (≠ I191)
- binding malonate ion: A120 (= A136), G122 (≠ S138), S146 (= S164), T167 (= T185), A168 (≠ S186), S170 (= S188), S193 (≠ R211), G194 (= G212), V195 (= V213), R200 (≠ P218), Y297 (≠ H309), R305 (≠ A317)
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 83% coverage: 78:465/470 of query aligns to 57:465/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 87% coverage: 56:463/470 of query aligns to 49:482/485 of 2f2aA
- active site: K79 (= K86), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (≠ S186), G177 (= G187), S178 (= S188), Q181 (≠ I191)
- binding glutamine: G130 (≠ S138), S154 (= S164), D174 (= D184), T175 (= T185), G176 (≠ S186), S178 (= S188), F206 (≠ L216), Y309 (≠ P298), Y310 (= Y299), R358 (= R340), D425 (≠ Y413)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 87% coverage: 56:463/470 of query aligns to 49:482/485 of 2dqnA
- active site: K79 (= K86), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (≠ S186), G177 (= G187), S178 (= S188), Q181 (≠ I191)
- binding asparagine: M129 (≠ F137), G130 (≠ S138), T175 (= T185), G176 (≠ S186), S178 (= S188), Y309 (≠ P298), Y310 (= Y299), R358 (= R340), D425 (≠ Y413)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
26% identity, 87% coverage: 58:467/470 of query aligns to 54:561/564 of 6te4A
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
40% identity, 35% coverage: 78:242/470 of query aligns to 73:238/487 of 1m21A
- active site: K81 (= K86), S160 (= S164), S161 (= S165), T179 (= T183), T181 (= T185), D182 (≠ S186), G183 (= G187), S184 (= S188), C187 (≠ I191)
- binding : A129 (= A136), N130 (vs. gap), F131 (= F137), C158 (≠ G162), G159 (= G163), S160 (= S164), S184 (= S188), C187 (≠ I191), I212 (≠ L216)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 82% coverage: 76:459/470 of query aligns to 52:412/412 of 1o9oA
- active site: K62 (= K86), A131 (vs. gap), S132 (= S165), T150 (= T183), T152 (= T185), G153 (≠ S186), G154 (= G187), S155 (= S188), R158 (≠ I191)
- binding 3-amino-3-oxopropanoic acid: G130 (vs. gap), T152 (= T185), G153 (≠ S186), G154 (= G187), S155 (= S188), R158 (≠ I191), P359 (≠ E395)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
24% identity, 81% coverage: 76:454/470 of query aligns to 85:497/508 of 3a1iA
- active site: K95 (= K86), S170 (≠ G162), S171 (≠ G163), G189 (≠ T183), Q191 (≠ T185), G192 (≠ S186), G193 (= G187), A194 (≠ S188), I197 (= I191)
- binding benzamide: F145 (= F137), S146 (= S138), G147 (= G139), Q191 (≠ T185), G192 (≠ S186), G193 (= G187), A194 (≠ S188), W327 (≠ H309)
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
27% identity, 80% coverage: 83:460/470 of query aligns to 66:457/593 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.
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 82% coverage: 76:459/470 of query aligns to 52:412/412 of 1ocmA
- active site: K62 (= K86), S131 (= S164), S132 (= S165), T152 (= T185), G153 (≠ S186), G154 (= G187), S155 (= S188)
- binding pyrophosphate 2-: R113 (≠ S138), S131 (= S164), Q151 (≠ D184), T152 (= T185), G153 (≠ S186), G154 (= G187), S155 (= S188), R158 (≠ I191), P359 (≠ E395)
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)
34% identity, 39% coverage: 23:207/470 of query aligns to 86:260/579 of Q9TUI8
- S217 (= S164) mutation to A: Loss of activity.
- S218 (= S165) mutation to A: Lowers activity by at least 98%.
- D237 (= D184) mutation D->E,N: Loss of activity.
- S241 (= S188) mutation to A: Loss of activity.
- C249 (= C196) mutation to A: Loss of activity.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
29% identity, 84% coverage: 50:446/470 of query aligns to 2:446/450 of 4n0iA
- active site: K38 (= K86), S116 (= S164), S117 (= S165), T135 (= T183), T137 (= T185), G138 (≠ S186), G139 (= G187), S140 (= S188), L143 (≠ I191)
- binding glutamine: G89 (≠ S138), T137 (= T185), G138 (≠ S186), S140 (= S188), Y168 (≠ L216), Y271 (≠ H309), Y272 (≠ G310), R320 (≠ K350), D404 (≠ N407)
Query Sequence
>GFF3601 FitnessBrowser__Marino:GFF3601
MRISEILREGALRSRIEALSFGMRSGRLSPVDVFRETRFKQGYSKNQGILVEPLGETSLA
QARSSEKRYLNDEQFGLLDGIPFGVKDLIDVEGCTTSRGSLLYRNAPPAKRNAEAVERLG
FQGMVFGGKTNLSELAFSGVGTNDLFGSPINPRATTGKYITGGSSSGSAAGVASGLWPVS
LGTDTSGSSRIPAAFCGVVGFKPSFDRYPLRGVAPLAPSLDHLGINALTVQDCVILDQAL
RGLAPIPKFRMLSEQTEFLVPRNKSIQPRDPHIKDNFDKTLDLLSNLGFEIHEVDFSPYA
EVDRLFEIHGSLVAHEAAQQYEALFENGLTSYIDPKILQRLKEGTLLNRKSYALLQKIRR
NLRAELSSSIGNKILLQPTVKILPPAIESVLKGVEEFKAFNKLILGNTMYANYLGMPAIA
IPIGHAPNGFSTSIQLSAASGKDDFLLKTALFLEAALSKQNIYTPDTVSH
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