SitesBLAST
Comparing GFF1302 FitnessBrowser__psRCH2:GFF1302 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)
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)
54% identity, 99% coverage: 6:562/563 of query aligns to 5:560/561 of P69451
- Y213 (= Y214) mutation to A: Loss of activity.
- T214 (= T215) mutation to A: 10% of wild-type activity.
- G216 (= G217) mutation to A: Decreases activity.
- T217 (= T218) mutation to A: Decreases activity.
- G219 (= G220) mutation to A: Decreases activity.
- K222 (= K223) mutation to A: Decreases activity.
- E361 (= E362) mutation to A: Loss of activity.
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)
30% identity, 98% coverage: 3:551/563 of query aligns to 15:536/546 of Q84P21
- K530 (= K545) mutation to N: Lossed enzymatic activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 90% coverage: 47:553/563 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T215), N183 (= N235), H207 (= H262), T303 (= T361), E304 (= E362), I403 (≠ L460), N408 (= N465), A491 (≠ K545)
- binding adenosine-5'-triphosphate: T163 (= T215), S164 (≠ G216), G165 (= G217), T166 (= T218), T167 (= T219), H207 (= H262), S277 (≠ G335), A278 (≠ M336), P279 (≠ A337), E298 (= E356), M302 (≠ L360), T303 (= T361), D382 (= D439), R397 (= R454)
- binding carbonate ion: H207 (= H262), S277 (≠ G335), R299 (≠ G357), G301 (= G359)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
32% identity, 90% coverage: 48:552/563 of query aligns to 47:534/539 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 (= H262), F245 (≠ Y264), T249 (≠ H269), G314 (= G335), A315 (≠ M336), P316 (≠ A337), G337 (= G357), Y338 (= Y358), G339 (= G359), L340 (= L360), T341 (= T361), S345 (≠ P365), A346 (≠ V366), D420 (= D439), I432 (= I451), K527 (= K545)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ Y264), R335 (≠ C355), G337 (= G357), G339 (= G359), L340 (= L360), A346 (≠ V366)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
32% identity, 90% coverage: 48:552/563 of query aligns to 47:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H262), F245 (≠ Y264), T249 (≠ H269), G314 (= G335), A315 (≠ M336), P316 (≠ A337), G337 (= G357), Y338 (= Y358), G339 (= G359), L340 (= L360), T341 (= T361), A346 (≠ V366), D420 (= D439), I432 (= I451), K527 (= K545)
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)
30% identity, 97% coverage: 6:552/563 of query aligns to 19:542/559 of Q67W82
- G395 (= G405) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 95% coverage: 25:558/563 of query aligns to 5:513/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 215:219) binding ATP
- H214 (= H262) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G335) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GMA 335:337) binding ATP
- EA 310:311 (≠ EG 356:357) binding ATP
- M314 (≠ L360) binding oxalate
- T315 (= T361) binding ATP
- H319 (≠ P365) binding oxalate; mutation to A: Abolished activity.
- D394 (= D439) binding ATP
- R409 (= R454) binding ATP; mutation to A: Abolished activity.
- K500 (= K545) binding ATP; binding oxalate; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
29% identity, 93% coverage: 25:549/563 of query aligns to 5:497/504 of 5ie3A
- active site: T163 (= T215), S183 (≠ N235), H207 (= H262), T308 (= T361), E309 (= E362), N408 (≠ L460), K413 (≠ N465), K493 (= K545)
- binding adenosine monophosphate: S164 (≠ G216), S282 (≠ G335), A283 (≠ M336), S284 (≠ A337), Y305 (= Y358), A306 (≠ G359), M307 (≠ L360), T308 (= T361), D387 (= D439), L399 (≠ I451), R402 (= R454), K493 (= K545)
- binding oxalic acid: V208 (≠ I263), S282 (≠ G335), A306 (≠ G359), M307 (≠ L360), H312 (≠ P365), K493 (= K545)
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 93% coverage: 25:549/563 of query aligns to 5:499/506 of 5ie2A
- active site: T165 (= T215), S185 (≠ N235), H209 (= H262), T310 (= T361), E311 (= E362), N410 (≠ L460), K415 (≠ N465), K495 (= K545)
- binding adenosine-5'-triphosphate: T165 (= T215), S166 (≠ G216), G167 (= G217), T168 (= T218), T169 (= T219), S284 (≠ G335), A285 (≠ M336), S286 (≠ A337), Y307 (= Y358), A308 (≠ G359), M309 (≠ L360), T310 (= T361), D389 (= D439), L401 (≠ I451), R404 (= R454), K495 (= K545)
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)
28% identity, 93% coverage: 32:552/563 of query aligns to 44:547/556 of Q9S725
- K211 (= K223) mutation to S: Drastically reduces the activity.
- M293 (≠ V305) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L332) mutation K->L,A: Affects the substrate specificity.
- E401 (= E406) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C408) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R454) mutation to Q: Drastically reduces the activity.
- K457 (≠ S462) mutation to S: Drastically reduces the activity.
- K540 (= K545) mutation to N: Abolishes the activity.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 95% coverage: 20:552/563 of query aligns to 9:525/528 of 5bsrA
- active site: S181 (≠ T215), S201 (≠ N235), H229 (= H262), T328 (= T361), E329 (= E362), K433 (≠ L460), Q438 (≠ N465), K518 (= K545)
- binding adenosine monophosphate: A301 (≠ G335), G326 (= G359), T328 (= T361), D412 (= D439), K429 (= K456), K433 (≠ L460), Q438 (≠ N465)
- binding coenzyme a: L102 (= L108), P226 (= P259), H229 (= H262), Y231 (= Y264), F253 (≠ R287), K435 (≠ S462), G436 (= G463), F437 (= F464), F498 (≠ G525)
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)
30% identity, 93% coverage: 32:552/563 of query aligns to 33:533/542 of O24146
- S189 (≠ T215) binding ATP
- S190 (≠ G216) binding ATP
- G191 (= G217) binding ATP
- T192 (= T218) binding ATP
- T193 (= T219) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K223) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H262) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y264) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ F268) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ P286) binding CoA
- A309 (≠ G335) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E356) binding ATP
- G332 (= G357) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T361) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V366) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ V369) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D439) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R454) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K456) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ L460) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S462) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G463) binding CoA
- Q446 (≠ N465) binding AMP
- K526 (= K545) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 95% coverage: 20:552/563 of query aligns to 10:526/529 of 5bsvA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L460), Q439 (≠ N465), K519 (= K545)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H262), Y232 (= Y264), S236 (≠ F268), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), G325 (= G357), G327 (= G359), M328 (≠ L360), T329 (= T361), P333 (= P365), V334 (= V366), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 95% coverage: 20:552/563 of query aligns to 10:526/529 of 5bsuA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L460), Q439 (≠ N465), K519 (= K545)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H262), Y232 (= Y264), S236 (≠ F268), M299 (≠ L332), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), G325 (= G357), G327 (= G359), M328 (≠ L360), T329 (= T361), P333 (= P365), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 95% coverage: 20:552/563 of query aligns to 10:526/529 of 5bstA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L460), Q439 (≠ N465), K519 (= K545)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H262), Y232 (= Y264), S236 (≠ F268), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), G325 (= G357), Y326 (= Y358), G327 (= G359), M328 (≠ L360), T329 (= T361), P333 (= P365), V334 (= V366), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 95% coverage: 20:552/563 of query aligns to 10:526/530 of 5bsmA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L460), Q439 (≠ N465), K519 (= K545)
- binding adenosine-5'-triphosphate: S182 (≠ T215), S183 (≠ G216), G184 (= G217), T185 (= T218), T186 (= T219), K190 (= K223), H230 (= H262), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), Y326 (= Y358), G327 (= G359), M328 (≠ L360), T329 (= T361), D413 (= D439), I425 (= I451), R428 (= R454), K519 (= K545)
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
30% identity, 91% coverage: 43:552/563 of query aligns to 58:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
30% identity, 95% coverage: 20:553/563 of query aligns to 13:533/539 of 2d1sA
- active site: S194 (≠ T215), R214 (≠ N235), H241 (= H262), T339 (= T361), E340 (= E362), K439 (≠ L460), Q444 (≠ N465), K525 (= K545)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T215), S195 (≠ G216), H241 (= H262), F243 (≠ Y264), T247 (≠ H269), I282 (≠ V305), G312 (= G335), A313 (≠ M336), P314 (≠ A337), Q334 (≠ E356), G335 (= G357), Y336 (= Y358), G337 (= G359), L338 (= L360), T339 (= T361), S343 (≠ P365), A344 (≠ V366), D418 (= D439), R433 (= R454), K525 (= K545)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
30% identity, 95% coverage: 20:553/563 of query aligns to 13:533/539 of 2d1rA
- active site: S194 (≠ T215), R214 (≠ N235), H241 (= H262), T339 (= T361), E340 (= E362), K439 (≠ L460), Q444 (≠ N465), K525 (= K545)
- binding adenosine monophosphate: S194 (≠ T215), S195 (≠ G216), H241 (= H262), G312 (= G335), A313 (≠ M336), P314 (≠ A337), G335 (= G357), Y336 (= Y358), G337 (= G359), L338 (= L360), T339 (= T361), D418 (= D439), K525 (= K545)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H262), F243 (≠ Y264), T247 (≠ H269), G335 (= G357), G337 (= G359), L338 (= L360), A344 (≠ V366)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
30% identity, 95% coverage: 20:552/563 of query aligns to 9:522/527 of 5u95B
Query Sequence
>GFF1302 FitnessBrowser__psRCH2:GFF1302
MTDNFWKDKYPVGVSSEINPDEYQNIQAVLKQSCERFADKPAFSNLGKTLTYGELYKLSG
DFAAYLQQNTDLQPGDRIAVQLPNLIQYPIVVFGAMRAGLIVVNTNPLYTAREMEHQFND
AGAKALVCLANMAHLAEEVLPKTGIKHVVITEVADMLPPLKRMLVNAVVKHVKKMVPAYS
LPKAVKLNDALALGRGKPVREALPKSDDVAVLQYTGGTTGVAKGAMLTHRNIVANMLQCK
ALMGSNLNDGSEVLIAPLPLYHIYAFTFHCMAMMLSGNHNILISNPRDLPAMIKDLGKYR
FSGFVGLNTLFVALCNSEDFRKLDFSALKVTLSGGMALQLATAERWKQVTGCPICEGYGL
TETSPVASVNPIEHIQLGSIGIPVPSTQFKVINDDGQDLAQGEIGELCIKGPQVMKGYWQ
RPEATDEVIDAQGWFKTGDIGVIQEDGYIRIVDRKKDMILVSGFNVYPNELEDVLASLPG
VLQSAAIGVPDEKSGEAIKLFVVVKPGESLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPT
TNVGKILRRELRDEELRKLGHKK
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