SitesBLAST
Comparing 3606823 FitnessBrowser__Dino:3606823 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)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
42% identity, 98% coverage: 3:512/519 of query aligns to 4:530/530 of 5bsmA
- active site: S182 (= S178), S202 (≠ N198), H230 (= H222), T329 (= T320), E330 (= E321), K434 (= K417), Q439 (= Q422), K519 (= K501)
- binding adenosine-5'-triphosphate: S182 (= S178), S183 (= S179), G184 (= G180), T185 (= T181), T186 (= T182), K190 (= K186), H230 (= H222), A302 (= A294), A303 (= A295), P304 (= P296), Y326 (= Y317), G327 (= G318), M328 (= M319), T329 (= T320), D413 (= D396), I425 (= I408), R428 (= R411), K519 (= K501)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
42% identity, 98% coverage: 3:511/519 of query aligns to 4:529/529 of 5bsvA
- active site: S182 (= S178), S202 (≠ N198), H230 (= H222), T329 (= T320), E330 (= E321), K434 (= K417), Q439 (= Q422), K519 (= K501)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H222), Y232 (= Y224), S236 (≠ V228), A302 (= A294), A303 (= A295), P304 (= P296), G325 (= G316), G327 (= G318), M328 (= M319), T329 (= T320), P333 (= P324), V334 (= V325), D413 (= D396), K430 (= K413), K434 (= K417), Q439 (= Q422)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
42% identity, 98% coverage: 3:511/519 of query aligns to 4:529/529 of 5bsuA
- active site: S182 (= S178), S202 (≠ N198), H230 (= H222), T329 (= T320), E330 (= E321), K434 (= K417), Q439 (= Q422), K519 (= K501)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H222), Y232 (= Y224), S236 (≠ V228), M299 (≠ L291), A302 (= A294), A303 (= A295), P304 (= P296), G325 (= G316), G327 (= G318), M328 (= M319), T329 (= T320), P333 (= P324), D413 (= D396), K430 (= K413), K434 (= K417), Q439 (= Q422)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
42% identity, 98% coverage: 3:511/519 of query aligns to 4:529/529 of 5bstA
- active site: S182 (= S178), S202 (≠ N198), H230 (= H222), T329 (= T320), E330 (= E321), K434 (= K417), Q439 (= Q422), K519 (= K501)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H222), Y232 (= Y224), S236 (≠ V228), A302 (= A294), A303 (= A295), P304 (= P296), G325 (= G316), Y326 (= Y317), G327 (= G318), M328 (= M319), T329 (= T320), P333 (= P324), V334 (= V325), D413 (= D396), K430 (= K413), K434 (= K417), Q439 (= Q422)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
42% identity, 98% coverage: 3:511/519 of query aligns to 3:528/528 of 5bsrA
- active site: S181 (= S178), S201 (≠ N198), H229 (= H222), T328 (= T320), E329 (= E321), K433 (= K417), Q438 (= Q422), K518 (= K501)
- binding adenosine monophosphate: A301 (= A294), G326 (= G318), T328 (= T320), D412 (= D396), K429 (= K413), K433 (= K417), Q438 (= Q422)
- binding coenzyme a: L102 (≠ T101), P226 (= P219), H229 (= H222), Y231 (= Y224), F253 (= F246), K435 (≠ S419), G436 (= G420), F437 (= F421), F498 (≠ H481)
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
42% identity, 98% coverage: 3:512/519 of query aligns to 11:537/542 of O24146
- S189 (= S178) binding
- S190 (= S179) binding
- G191 (= G180) binding
- T192 (= T181) binding
- T193 (= T182) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K186) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H222) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y224) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V228) binding ; binding ; binding
- K260 (≠ R245) binding
- A309 (= A294) binding ; binding ; binding
- Q331 (= Q315) binding
- G332 (= G316) binding ; binding ; binding ; binding ; binding
- T336 (= T320) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V325) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (vs. gap) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D396) binding ; binding ; binding ; binding ; binding
- R435 (= R411) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K413) binding ; binding ; binding ; binding
- K441 (= K417) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S419) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G420) binding
- Q446 (= Q422) binding
- K526 (= K501) binding ; mutation to A: Abolished activity against 4-coumarate.
Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
39% identity, 98% coverage: 3:513/519 of query aligns to 22:552/556 of Q9S725
- K211 (= K186) mutation to S: Drastically reduces the activity.
- M293 (≠ Y264) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L291) mutation K->L,A: Affects the substrate specificity.
- E401 (= E363) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ W365) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R411) mutation to Q: Drastically reduces the activity.
- K457 (≠ S419) mutation to S: Drastically reduces the activity.
- K540 (= K501) mutation to N: Abolishes the activity.
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
42% identity, 98% coverage: 3:512/519 of query aligns to 3:526/527 of 5u95B
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
41% identity, 98% coverage: 3:510/519 of query aligns to 4:528/528 of 3ni2A
- active site: S182 (= S178), S202 (≠ N198), H230 (= H222), T329 (= T320), E330 (= E321), K434 (= K417), Q439 (= Q422), K519 (= K501)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y224), S236 (≠ V228), G302 (≠ A294), A303 (= A295), P304 (= P296), G325 (= G316), G327 (= G318), T329 (= T320), P333 (= P324), V334 (= V325), D413 (= D396), K430 (= K413), K434 (= K417), Q439 (= Q422)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
41% identity, 98% coverage: 3:510/519 of query aligns to 4:528/528 of 3a9vA
- active site: S182 (= S178), S202 (≠ N198), H230 (= H222), T329 (= T320), E330 (= E321), K434 (= K417), Q439 (= Q422), K519 (= K501)
- binding adenosine monophosphate: H230 (= H222), G302 (≠ A294), A303 (= A295), P304 (= P296), Y326 (= Y317), G327 (= G318), M328 (= M319), T329 (= T320), D413 (= D396), K430 (= K413), K434 (= K417), Q439 (= Q422)
Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
40% identity, 99% coverage: 3:518/519 of query aligns to 18:552/559 of Q67W82
- G395 (= G362) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 91% coverage: 35:507/519 of query aligns to 49:536/546 of Q84P21
- K530 (= K501) mutation to N: Lossed enzymatic activity.
7kydA Drosophila melanogaster long-chain fatty-acyl-coa synthetase cg6178 (see paper)
35% identity, 97% coverage: 3:508/519 of query aligns to 10:530/534 of 7kydA
- binding 5'-O-[(S)-hydroxy(octanoyloxy)phosphoryl]adenosine: H240 (= H222), F242 (≠ Y224), A311 (= A294), A312 (= A295), P313 (= P296), G334 (= G316), Y335 (= Y317), G336 (= G318), L337 (≠ M319), S338 (≠ T320), S343 (= S326), D416 (= D396), I428 (= I408)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
34% identity, 94% coverage: 20:508/519 of query aligns to 22:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H222), F245 (≠ Y224), T249 (≠ V228), G314 (≠ A294), A315 (= A295), P316 (= P296), G337 (= G316), Y338 (= Y317), G339 (= G318), L340 (≠ M319), T341 (= T320), A346 (≠ V325), D420 (= D396), I432 (= I408), K527 (= K501)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
34% identity, 94% coverage: 20:508/519 of query aligns to 22:534/539 of 6k4dA
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (= H222), F245 (≠ Y224), T249 (≠ V228), G314 (≠ A294), A315 (= A295), P316 (= P296), G337 (= G316), Y338 (= Y317), G339 (= G318), L340 (≠ M319), T341 (= T320), S345 (≠ P324), A346 (≠ V325), D420 (= D396), I432 (= I408), K527 (= K501)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ Y224), R335 (vs. gap), G337 (= G316), G339 (= G318), L340 (≠ M319), A346 (≠ V325)
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
34% identity, 95% coverage: 14:508/519 of query aligns to 21:550/561 of P69451
- Y213 (= Y177) mutation to A: Loss of activity.
- T214 (≠ S178) mutation to A: 10% of wild-type activity.
- G216 (= G180) mutation to A: Decreases activity.
- T217 (= T181) mutation to A: Decreases activity.
- G219 (= G183) mutation to A: Decreases activity.
- K222 (= K186) mutation to A: Decreases activity.
- E361 (= E321) mutation to A: Loss of activity.
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
36% identity, 88% coverage: 54:508/519 of query aligns to 55:532/539 of 2d1sA
- active site: S194 (= S178), R214 (≠ N198), H241 (= H222), T339 (= T320), E340 (= E321), K439 (= K417), Q444 (= Q422), K525 (= K501)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (= S178), S195 (= S179), H241 (= H222), F243 (≠ Y224), T247 (≠ V228), I282 (≠ Y264), G312 (≠ A294), A313 (= A295), P314 (= P296), Q334 (= Q315), G335 (= G316), Y336 (= Y317), G337 (= G318), L338 (≠ M319), T339 (= T320), S343 (≠ P324), A344 (≠ V325), D418 (= D396), R433 (= R411), K525 (= K501)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
36% identity, 88% coverage: 54:508/519 of query aligns to 55:532/539 of 2d1rA
- active site: S194 (= S178), R214 (≠ N198), H241 (= H222), T339 (= T320), E340 (= E321), K439 (= K417), Q444 (= Q422), K525 (= K501)
- binding adenosine monophosphate: S194 (= S178), S195 (= S179), H241 (= H222), G312 (≠ A294), A313 (= A295), P314 (= P296), G335 (= G316), Y336 (= Y317), G337 (= G318), L338 (≠ M319), T339 (= T320), D418 (= D396), K525 (= K501)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H222), F243 (≠ Y224), T247 (≠ V228), G335 (= G316), G337 (= G318), L338 (≠ M319), A344 (≠ V325)
6q2mA Crystal structure of photinus pyralis luciferase pps6 mutant in complex with dlsa (see paper)
34% identity, 91% coverage: 39:508/519 of query aligns to 36:535/544 of 6q2mA
- active site: S197 (= S178), R217 (≠ N198), H244 (= H222), T342 (= T320), E343 (= E321), K442 (= K417), Q447 (= Q422), K528 (= K501)
- binding (2S,5S)-hexane-2,5-diol: D186 (= D167), R187 (≠ L168), R260 (≠ A239), Y279 (≠ H258)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S198 (= S179), H244 (= H222), F246 (≠ Y224), T250 (≠ V228), G315 (≠ A294), A316 (= A295), P317 (= P296), G338 (= G316), Y339 (= Y317), G340 (= G318), L341 (≠ M319), T342 (= T320), S346 (≠ P324), A347 (≠ V325), D421 (= D396), K528 (= K501)
Sites not aligning to the query:
6hpsA Near-infrared dual bioluminescence imaging in vivo using infra- luciferin (see paper)
34% identity, 91% coverage: 39:508/519 of query aligns to 33:532/539 of 6hpsA
- active site: S194 (= S178), R214 (≠ N198), H241 (= H222), T339 (= T320), E340 (= E321), K439 (= K417), Q444 (= Q422), K525 (= K501)
- binding [(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl ~{N}-[[2-[(~{E})-2-(6-oxidanyl-1,3-benzothiazol-2-yl)ethenyl]-1,3-thiazol-4-yl]carbonyl]sulfamate: H241 (= H222), G242 (≠ I223), F243 (≠ Y224), S310 (= S292), G312 (≠ A294), A313 (= A295), P314 (= P296), R333 (vs. gap), G335 (= G316), Y336 (= Y317), G337 (= G318), L338 (≠ M319), T339 (= T320), A344 (≠ V325), D418 (= D396), K525 (= K501)
Query Sequence
>3606823 FitnessBrowser__Dino:3606823
MKIYRSPFADVTVRDLSITEALFEGLARRGDAPILIDGPSGAAMTGAQLEGRIRACAGGL
RARGIGPGDVVAIMAPNMPDYATAFHGAAFAGATVTTLNPTYTTEEAAHQLRDSGAQMLV
TVPAFADLAAEAVQGTGVTETVMMGTTGPGSLEALFGPPLAAQVAVDLARDIVVLPYSSG
TTGLPKGVMLSHRNLVVNVDQTAEIIGITVQDVTVGFLPFFHIYGMTVLMNCYLSRGAAV
VTMPRFDLEQFLSLCQTHRPRQLYIAPPVALALAKHPMVDDYDLSGVEFILSGAAPLGGD
VAEAVGRRLGVEMVQGYGMTEMSPVSHFTPPGQNVPGSVGPTAPSAESRIVDPETGEDAA
EGEVWVRGPQIMQGYLNRPDATAETVTRDGWLKTGDLGRFDEAGNLFITDRVKELIKVSG
FQVAPAELEAVLLTHPAITDAAVIGVPDDSAGERPMAFVVRSDPDLSEGAVIAHAAEHLA
HYKRIARVAFVEAVPKSASGKILRRLLRAKVGEDMATGA
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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