SitesBLAST
Comparing RR42_RS26915 FitnessBrowser__Cup4G11:RR42_RS26915 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)
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)
41% identity, 95% coverage: 17:560/573 of query aligns to 23:571/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
32% identity, 92% coverage: 36:560/573 of query aligns to 28:551/561 of P69451
- Y213 (≠ F221) mutation to A: Loss of activity.
- T214 (= T222) mutation to A: 10% of wild-type activity.
- G216 (= G224) mutation to A: Decreases activity.
- T217 (= T225) mutation to A: Decreases activity.
- G219 (= G227) mutation to A: Decreases activity.
- K222 (= K230) mutation to A: Decreases activity.
- E361 (= E367) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 88% coverage: 56:560/573 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T222), N183 (= N242), H207 (= H266), T303 (= T366), E304 (= E367), I403 (= I467), N408 (= N472), A491 (≠ K552)
- binding adenosine-5'-triphosphate: T163 (= T222), S164 (= S223), G165 (= G224), T166 (= T225), T167 (= T226), H207 (= H266), S277 (≠ G339), A278 (≠ S340), P279 (= P341), E298 (≠ I361), M302 (= M365), T303 (= T366), D382 (= D446), R397 (= R461)
- binding carbonate ion: H207 (= H266), S277 (≠ G339), R299 (≠ A362), G301 (= G364)
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
29% identity, 91% coverage: 45:563/573 of query aligns to 16:498/503 of P9WQ37
- R17 (≠ D46) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K230) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S253) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q255) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C267) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (≠ G269) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L272) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (= R304) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G364) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (= W441) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D446) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (= R461) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R468) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G470) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K552) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
30% identity, 95% coverage: 23:568/573 of query aligns to 3:518/518 of 4wv3B
- active site: S175 (≠ T222), T320 (= T366), E321 (= E367), K418 (≠ I467), W423 (≠ N472), K502 (= K552)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H266), T221 (≠ C267), F222 (= F268), A293 (= A338), S294 (≠ G339), E295 (≠ S340), A296 (≠ P341), G316 (≠ A362), I317 (≠ Y363), G318 (= G364), C319 (≠ M365), T320 (= T366), D397 (= D446), H409 (≠ I458), R412 (= R461), K502 (= K552)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
27% identity, 90% coverage: 32:546/573 of query aligns to 5:493/504 of 6qjzA
- active site: T169 (= T222), S189 (≠ N242), H213 (= H266), T314 (= T366), E315 (= E367), N414 (≠ I467), K419 (≠ N472)
- binding adenosine monophosphate: H213 (= H266), S288 (≠ I336), A289 (≠ M337), S290 (≠ A338), A312 (≠ G364), M313 (= M365), T314 (= T366), D393 (= D446), L405 (≠ I458), K410 (= K463), K419 (≠ N472)
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)
27% identity, 93% coverage: 32:562/573 of query aligns to 5:510/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 222:226) binding
- H214 (= H266) binding ; mutation to A: Abolished activity.
- S289 (≠ I336) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ IMA 336:338) binding
- EA 310:311 (≠ IA 361:362) binding
- M314 (= M365) binding
- T315 (= T366) binding
- H319 (≠ P370) binding ; mutation to A: Abolished activity.
- D394 (= D446) binding
- R409 (= R461) binding ; mutation to A: Abolished activity.
- K500 (= K552) binding ; binding ; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
27% identity, 93% coverage: 32:562/573 of query aligns to 5:503/504 of 5ie3A
- active site: T163 (= T222), S183 (≠ N242), H207 (= H266), T308 (= T366), E309 (= E367), N408 (≠ I467), K413 (≠ N472), K493 (= K552)
- binding adenosine monophosphate: S164 (= S223), S282 (≠ I336), A283 (≠ M337), S284 (≠ A338), Y305 (= Y363), A306 (≠ G364), M307 (= M365), T308 (= T366), D387 (= D446), L399 (≠ I458), R402 (= R461), K493 (= K552)
- binding oxalic acid: V208 (≠ C267), S282 (≠ I336), A306 (≠ G364), M307 (= M365), H312 (≠ P370), K493 (= K552)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
28% identity, 91% coverage: 45:563/573 of query aligns to 19:498/502 of 3r44A
Sites not aligning to the query:
5ie2A Crystal structure of a plant enzyme (see paper)
27% identity, 93% coverage: 32:562/573 of query aligns to 5:505/506 of 5ie2A
- active site: T165 (= T222), S185 (≠ N242), H209 (= H266), T310 (= T366), E311 (= E367), N410 (≠ I467), K415 (≠ N472), K495 (= K552)
- binding adenosine-5'-triphosphate: T165 (= T222), S166 (= S223), G167 (= G224), T168 (= T225), T169 (= T226), S284 (≠ I336), A285 (≠ M337), S286 (≠ A338), Y307 (= Y363), A308 (≠ G364), M309 (= M365), T310 (= T366), D389 (= D446), L401 (≠ I458), R404 (= R461), K495 (= K552)
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)
26% identity, 91% coverage: 39:562/573 of query aligns to 44:550/556 of Q9S725
- K211 (= K230) mutation to S: Drastically reduces the activity.
- M293 (≠ H309) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I336) mutation K->L,A: Affects the substrate specificity.
- E401 (= E414) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C416) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R461) mutation to Q: Drastically reduces the activity.
- K457 (≠ G469) mutation to S: Drastically reduces the activity.
- K540 (= K552) mutation to N: Abolishes the 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)
26% identity, 88% coverage: 47:553/573 of query aligns to 46:531/546 of Q84P21
- K530 (= K552) mutation to N: Lossed enzymatic activity.
P38137 Oxalate--CoA ligase; Acyl-activating enzyme 3; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 93% coverage: 29:560/573 of query aligns to 3:531/543 of P38137
Sites not aligning to the query:
- 541:543 C-terminal peroxisome targeting signal (PTS1)
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
28% identity, 93% coverage: 31:562/573 of query aligns to 6:533/539 of P0DX84
- H231 (= H266) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ M270) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A338) mutation to P: Almost completely abolishes the activity.
- G303 (= G339) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y363) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P370) mutation to A: Retains 69% of wild-type activity.
- R432 (= R461) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K463) mutation to A: Retains 36% of wild-type activity.
- D435 (= D464) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I467) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G469) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G470) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E471) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N472) mutation to A: Retains 60% of wild-type activity.
- E474 (= E503) mutation to A: Retains 33% of wild-type activity.
- K523 (= K552) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K555) mutation to A: Retains 48% of wild-type activity.
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
27% identity, 87% coverage: 60:560/573 of query aligns to 50:535/539 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 (= H266), F245 (= F268), T249 (≠ A273), G314 (= G339), A315 (≠ S340), P316 (= P341), G337 (≠ A362), Y338 (= Y363), G339 (= G364), L340 (≠ M365), T341 (= T366), S345 (≠ P370), A346 (≠ V371), D420 (= D446), I432 (= I458), K527 (= K552)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F268), R335 (≠ T360), G337 (≠ A362), G339 (= G364), L340 (≠ M365), A346 (≠ V371)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
27% identity, 87% coverage: 60:560/573 of query aligns to 50:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H266), F245 (= F268), T249 (≠ A273), G314 (= G339), A315 (≠ S340), P316 (= P341), G337 (≠ A362), Y338 (= Y363), G339 (= G364), L340 (≠ M365), T341 (= T366), A346 (≠ V371), D420 (= D446), I432 (= I458), K527 (= K552)
O74976 Oxalate--CoA ligase; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 83% coverage: 78:555/573 of query aligns to 47:497/512 of O74976
- S283 (≠ G339) modified: Phosphoserine
- S284 (= S340) modified: Phosphoserine
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
29% identity, 93% coverage: 30:561/573 of query aligns to 17:533/541 of Q5SKN9
- T184 (= T222) binding
- G302 (= G339) binding
- Q322 (≠ I361) binding
- G323 (≠ A362) binding
- T327 (= T366) binding
- E328 (= E367) binding
- D418 (= D446) binding
- K435 (= K463) binding
- K439 (≠ I467) binding
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
28% identity, 93% coverage: 31:562/573 of query aligns to 6:533/538 of 6ijbB
- active site: T185 (= T222), H205 (vs. gap), H231 (= H266), S329 (≠ T366), E330 (= E367), K438 (≠ I467), W443 (≠ N472), A523 (≠ K552)
- binding 3-(methylsulfanyl)propanoic acid: W235 (≠ M270), G303 (= G339), A325 (= A362), W326 (≠ Y363), G327 (= G364), M328 (= M365)
- binding adenosine monophosphate: G303 (= G339), A304 (≠ S340), A305 (≠ P341), H324 (≠ I361), W326 (≠ Y363), G327 (= G364), M328 (= M365), S329 (≠ T366), Q359 (vs. gap), D417 (= D446)
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
28% identity, 93% coverage: 27:560/573 of query aligns to 13:533/539 of 2d1sA
- active site: S194 (≠ T222), R214 (vs. gap), H241 (= H266), T339 (= T366), E340 (= E367), K439 (≠ I467), Q444 (≠ N472), K525 (= K552)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T222), S195 (= S223), H241 (= H266), F243 (= F268), T247 (vs. gap), I282 (≠ H309), G312 (= G339), A313 (≠ S340), P314 (= P341), Q334 (≠ I361), G335 (≠ A362), Y336 (= Y363), G337 (= G364), L338 (≠ M365), T339 (= T366), S343 (≠ P370), A344 (≠ V371), D418 (= D446), R433 (= R461), K525 (= K552)
Query Sequence
>RR42_RS26915 FitnessBrowser__Cup4G11:RR42_RS26915
MTMQGAASPTILPIGGLSHVRGSTDIPLSELTVPALLAETVARFPDREAVVFREQGIRWS
WREFAQVVDAMAGGLRLLGLERGDRIGIWSPNRVEWLVTQFATARLGLVLVNINPAYRLA
ELEYALNKVGCKAIVAAESFKTSRYLEMLQTLAPELKSCEPGTLQAARLPALRWVIRMGA
ERTPGMLNYDALLAHGTHALTSELDALTAQLDRYDPINIQFTSGTTGAPKGATLTHRNIV
NNARFIAMAMRFSEQDKLCIPVPFYHCFGMVLAVLACVSTGACMVFPGEAFEPAATMAAV
SEERCTALHGVPTMFIAQLDHPDFAKYDFSTLRTGIMAGSPCPIETMKRVISQMHMAQVT
IAYGMTETSPVSFQSSTTDPLDKRVTTVGQIQPHLEVKLVDGTGEIVPVGEKGELCTRGY
SVMQGYWDDEPRTREAIRDGWMHTGDLATIDAEGYCNIVGRVKDMLIRGGENVYPREIEE
FLFRHPKVQAVQVFGVPDPKYGEEVCAWIVLKPGDTATEDDIRAFCRDQIAHYKIPRYIR
FVDEMPMTITGKVQKFVMRERMTLELGLGDKTT
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