SitesBLAST
Comparing GFF3986 FitnessBrowser__Marino:GFF3986 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)
32% identity, 98% coverage: 7:548/554 of query aligns to 3:552/561 of P69451
- Y213 (= Y206) mutation to A: Loss of activity.
- T214 (≠ S207) mutation to A: 10% of wild-type activity.
- G216 (= G209) mutation to A: Decreases activity.
- T217 (= T210) mutation to A: Decreases activity.
- G219 (= G212) mutation to A: Decreases activity.
- K222 (= K215) mutation to A: Decreases activity.
- E361 (= E350) mutation to A: Loss of activity.
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
30% identity, 90% coverage: 48:547/554 of query aligns to 49:535/539 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 (= H251), F245 (≠ T253), T249 (≠ G257), G314 (= G323), A315 (= A324), P316 (≠ T325), G337 (= G345), Y338 (= Y346), G339 (= G347), L340 (= L348), T341 (≠ S349), S345 (≠ A353), A346 (= A354), D420 (= D431), I432 (≠ M443), K527 (= K539)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ T253), R335 (vs. gap), G337 (= G345), G339 (= G347), L340 (= L348), A346 (= A354)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
30% identity, 90% coverage: 48:547/554 of query aligns to 49:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H251), F245 (≠ T253), T249 (≠ G257), G314 (= G323), A315 (= A324), P316 (≠ T325), G337 (= G345), Y338 (= Y346), G339 (= G347), L340 (= L348), T341 (≠ S349), A346 (= A354), D420 (= D431), I432 (≠ M443), K527 (= K539)
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
29% identity, 95% coverage: 23:547/554 of query aligns to 18:533/539 of 2d1sA
- active site: S194 (= S207), R214 (≠ T227), H241 (= H251), T339 (≠ S349), E340 (= E350), K439 (≠ N452), Q444 (≠ K457), K525 (= K539)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (= S207), S195 (= S208), H241 (= H251), F243 (≠ T253), T247 (≠ G257), I282 (≠ T293), G312 (= G323), A313 (= A324), P314 (≠ T325), Q334 (≠ E344), G335 (= G345), Y336 (= Y346), G337 (= G347), L338 (= L348), T339 (≠ S349), S343 (≠ A353), A344 (= A354), D418 (= D431), R433 (= R446), K525 (= K539)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
29% identity, 95% coverage: 23:547/554 of query aligns to 18:533/539 of 2d1rA
- active site: S194 (= S207), R214 (≠ T227), H241 (= H251), T339 (≠ S349), E340 (= E350), K439 (≠ N452), Q444 (≠ K457), K525 (= K539)
- binding adenosine monophosphate: S194 (= S207), S195 (= S208), H241 (= H251), G312 (= G323), A313 (= A324), P314 (≠ T325), G335 (= G345), Y336 (= Y346), G337 (= G347), L338 (= L348), T339 (≠ S349), D418 (= D431), K525 (= K539)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H251), F243 (≠ T253), T247 (≠ G257), G335 (= G345), G337 (= G347), L338 (= L348), A344 (= A354)
6q2mA Crystal structure of photinus pyralis luciferase pps6 mutant in complex with dlsa (see paper)
30% identity, 93% coverage: 41:554/554 of query aligns to 39:543/544 of 6q2mA
- active site: S197 (= S207), R217 (≠ T227), H244 (= H251), T342 (≠ S349), E343 (= E350), K442 (≠ N452), Q447 (≠ K457), K528 (= K539)
- binding (2S,5S)-hexane-2,5-diol: D186 (≠ T197), R187 (≠ P198), R260 (≠ A268), Y279 (= Y287)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S198 (= S208), H244 (= H251), F246 (≠ T253), T250 (≠ G257), G315 (= G323), A316 (= A324), P317 (≠ T325), G338 (= G345), Y339 (= Y346), G340 (= G347), L341 (= L348), T342 (≠ S349), S346 (≠ A353), A347 (= A354), D421 (= D431), K528 (= K539)
Sites not aligning to the query:
6hpsA Near-infrared dual bioluminescence imaging in vivo using infra- luciferin (see paper)
30% identity, 93% coverage: 41:553/554 of query aligns to 36:539/539 of 6hpsA
- active site: S194 (= S207), R214 (≠ T227), H241 (= H251), T339 (≠ S349), E340 (= E350), K439 (≠ N452), Q444 (≠ K457), K525 (= K539)
- 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 (= H251), G242 (≠ V252), F243 (≠ T253), S310 (≠ G321), G312 (= G323), A313 (= A324), P314 (≠ T325), R333 (vs. gap), G335 (= G345), Y336 (= Y346), G337 (= G347), L338 (= L348), T339 (≠ S349), A344 (= A354), D418 (= D431), K525 (= K539)
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)
28% identity, 91% coverage: 41:545/554 of query aligns to 47:536/546 of Q84P21
- K530 (= K539) mutation to N: Lossed enzymatic activity.
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)
27% identity, 90% coverage: 49:546/554 of query aligns to 65:547/556 of Q9S725
- K211 (= K215) mutation to S: Drastically reduces the activity.
- M293 (≠ T293) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ G320) mutation K->L,A: Affects the substrate specificity.
- E401 (= E395) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V397) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R446) mutation to Q: Drastically reduces the activity.
- K457 (≠ S454) mutation to S: Drastically reduces the activity.
- K540 (= K539) mutation to N: Abolishes the activity.
1ba3A Firefly luciferase in complex with bromoform (see paper)
30% identity, 93% coverage: 41:554/554 of query aligns to 38:540/540 of 1ba3A
- active site: S196 (= S207), R214 (≠ T227), H241 (= H251), T339 (≠ S349), E340 (= E350), K439 (≠ N452), Q444 (≠ K457), K525 (= K539)
- binding tribromomethane: E307 (≠ M318), G311 (= G322), R333 (vs. gap), R333 (vs. gap), T348 (≠ N358), E350 (≠ N360)
5wysA Luciferase with inhibitor 3i (see paper)
30% identity, 93% coverage: 41:553/554 of query aligns to 38:539/539 of 5wysA
- active site: S196 (= S207), R214 (≠ T227), H241 (= H251), T339 (≠ S349), E340 (= E350), K439 (≠ N452), Q444 (≠ K457), K525 (= K539)
- binding 5-[(3R)-3-(4-boranylphenyl)-3-oxidanyl-propyl]-2-oxidanyl-benzoic acid: R214 (≠ T227), F243 (≠ T253), E307 (≠ M318), A309 (≠ G320), G311 (= G322), G312 (= G323), R333 (vs. gap), T342 (≠ M352), S343 (≠ A353), A344 (= A354)
Q17577 Acyl-CoA synthetase 7; EC 6.2.1.- from Caenorhabditis elegans (see paper)
27% identity, 94% coverage: 28:547/554 of query aligns to 23:530/540 of Q17577
- SS 186:187 (= SS 207:208) mutation to AA: Loss of catalytic activity; when associated with A-339.
- E339 (= E350) mutation to A: Severe loss of catalytic activity. Loss of catalytic activity; when associated with 186-A-A-187.
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)
28% identity, 97% coverage: 12:546/554 of query aligns to 27:542/559 of Q67W82
- G395 (= G394) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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: 45:548/554 of query aligns to 27:496/503 of P9WQ37
- K172 (= K215) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S241) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q243) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V252) 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 (≠ G254) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ G257) 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 (= R286) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G347) 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 (≠ F426) 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 (= D431) 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 (= R446) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ A453) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G455) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K539) 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.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
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, 94% coverage: 28:547/554 of query aligns to 10:508/514 of Q9SMT7
- TSGTT 170:174 (≠ SSGTT 207:211) binding
- H214 (= H251) binding ; mutation to A: Abolished activity.
- S289 (≠ G323) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAT 323:325) binding
- EA 310:311 (≠ EG 344:345) binding
- M314 (≠ L348) binding
- T315 (≠ S349) binding
- H319 (= H356) binding ; mutation to A: Abolished activity.
- D394 (= D431) binding
- R409 (= R446) binding ; mutation to A: Abolished activity.
- K500 (= K539) binding ; binding ; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
29% identity, 94% coverage: 28:547/554 of query aligns to 10:501/504 of 5ie3A
- active site: T163 (≠ S207), S183 (≠ A228), H207 (= H251), T308 (≠ S349), E309 (= E350), N408 (= N452), K413 (= K457), K493 (= K539)
- binding adenosine monophosphate: S164 (= S208), S282 (≠ G323), A283 (= A324), S284 (≠ T325), Y305 (= Y346), A306 (≠ G347), M307 (≠ L348), T308 (≠ S349), D387 (= D431), L399 (≠ M443), R402 (= R446), K493 (= K539)
- binding oxalic acid: V208 (= V252), S282 (≠ G323), A306 (≠ G347), M307 (≠ L348), H312 (= H356), K493 (= K539)
7kydA Drosophila melanogaster long-chain fatty-acyl-coa synthetase cg6178 (see paper)
28% identity, 89% coverage: 53:547/554 of query aligns to 57:531/534 of 7kydA
- binding 5'-O-[(S)-hydroxy(octanoyloxy)phosphoryl]adenosine: H240 (= H251), F242 (≠ T253), A311 (≠ G323), A312 (= A324), P313 (≠ T325), G334 (= G345), Y335 (= Y346), G336 (= G347), L337 (= L348), S338 (= S349), S343 (≠ A354), D416 (= D431), I428 (≠ M443)
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 94% coverage: 28:547/554 of query aligns to 10:503/506 of 5ie2A
- active site: T165 (≠ S207), S185 (≠ A228), H209 (= H251), T310 (≠ S349), E311 (= E350), N410 (= N452), K415 (= K457), K495 (= K539)
- binding adenosine-5'-triphosphate: T165 (≠ S207), S166 (= S208), G167 (= G209), T168 (= T210), T169 (= T211), S284 (≠ G323), A285 (= A324), S286 (≠ T325), Y307 (= Y346), A308 (≠ G347), M309 (≠ L348), T310 (≠ S349), D389 (= D431), L401 (≠ M443), R404 (= R446), K495 (= K539)
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)
27% identity, 90% coverage: 45:543/554 of query aligns to 25:498/512 of O74976
- S283 (≠ G323) modified: Phosphoserine
- S284 (≠ A324) modified: Phosphoserine
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
26% identity, 91% coverage: 43:548/554 of query aligns to 48:528/528 of 3ni2A
- active site: S182 (= S207), S202 (≠ T227), H230 (= H251), T329 (≠ S349), E330 (= E350), K434 (≠ N452), Q439 (≠ K457), K519 (= K539)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ T253), S236 (≠ G257), G302 (= G323), A303 (= A324), P304 (≠ T325), G325 (= G345), G327 (= G347), T329 (≠ S349), P333 (vs. gap), V334 (vs. gap), D413 (= D431), K430 (= K448), K434 (≠ N452), Q439 (≠ K457)
Query Sequence
>GFF3986 FitnessBrowser__Marino:GFF3986
MFDRHYKVWPKELPKTMTLPKTSVYTNLEISARRYPDHTAIIFYDAPITYRRLNEEVETL
AGYLQEQGVKKGDRVLLYMQNSPQYVISYYAILRADAVVIPVNPMNRSAELEHFIADTGA
TVCLAGQELAGFIAPMIGDSNLDQVVVASYSTYIDPETDLDLPAEVAAPVWSRDLPGVVT
WEVAMAAGYAPGPHTATPDDLAVIPYSSGTTGAPKGCMHTHRSVMATAIHRIFWNLTTPD
SVQLATLPFFHVTGMTGSMNGPIAAGAASVIMTRWDRTTASRLIERYKVTGWTNIVTMAV
DFLSNPDIGQYDLSSLNMIGGGGATMPSAVAEKLKRMTGLDYIEGYGLSETMAATHINPN
AHPKSQCLGIPVFDVDSRIIDVDTLEEKGPGETGEIVSCGPQVTRGYWNRPSETEAAFVE
IDGKQFFRTGDLGYYDEDGYFFMVDRVKRMINASGYKVWPSEVEGMMYRHPAIHEVCIIS
APDPKRGETVKACIVLTPEAEGQTSAGDIIAWCKEQMATYKVPTMIDFVDQLPKSPTGKL
MWRALQEEEWKEKS
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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