SitesBLAST
Comparing Pf1N1B4_572 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_572 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)
57% identity, 99% coverage: 1:337/341 of query aligns to 225:560/561 of P69451
- E361 (= E137) mutation to A: Loss of activity.
Sites not aligning to the query:
- 213 Y→A: Loss of activity.
- 214 T→A: 10% of wild-type activity.
- 216 G→A: Decreases activity.
- 217 T→A: Decreases activity.
- 219 G→A: Decreases activity.
- 222 K→A: Decreases activity.
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
34% identity, 96% coverage: 1:327/341 of query aligns to 207:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H37), F245 (≠ Y39), T249 (≠ H44), G314 (= G110), A315 (≠ M111), P316 (≠ A112), G337 (= G132), Y338 (= Y133), G339 (= G134), L340 (≠ M135), T341 (= T136), A346 (≠ V141), D420 (= D214), I432 (= I226), K527 (= K320)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
34% identity, 96% coverage: 1:327/341 of query aligns to 207:534/539 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 (= H37), F245 (≠ Y39), T249 (≠ H44), G314 (= G110), A315 (≠ M111), P316 (≠ A112), G337 (= G132), Y338 (= Y133), G339 (= G134), L340 (≠ M135), T341 (= T136), S345 (≠ P140), A346 (≠ V141), D420 (= D214), I432 (= I226), K527 (= K320)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ Y39), R335 (≠ C130), G337 (= G132), G339 (= G134), L340 (≠ M135), A346 (≠ V141)
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)
33% identity, 95% coverage: 3:326/341 of query aligns to 210:536/546 of Q84P21
- K530 (= K320) mutation to N: Lossed enzymatic activity.
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
34% identity, 97% coverage: 2:333/341 of query aligns to 206:537/539 of 2d1sA
- active site: R214 (≠ N10), H241 (= H37), T339 (= T136), E340 (= E137), K439 (≠ L235), Q444 (≠ N240), K525 (= K320)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H241 (= H37), F243 (≠ Y39), T247 (≠ H44), I282 (≠ V80), G312 (= G110), A313 (≠ M111), P314 (≠ A112), Q334 (≠ E131), G335 (= G132), Y336 (= Y133), G337 (= G134), L338 (≠ M135), T339 (= T136), S343 (≠ P140), A344 (≠ V141), D418 (= D214), R433 (= R229), K525 (= K320)
Sites not aligning to the query:
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
34% identity, 97% coverage: 2:333/341 of query aligns to 206:537/539 of 2d1rA
- active site: R214 (≠ N10), H241 (= H37), T339 (= T136), E340 (= E137), K439 (≠ L235), Q444 (≠ N240), K525 (= K320)
- binding adenosine monophosphate: H241 (= H37), G312 (= G110), A313 (≠ M111), P314 (≠ A112), G335 (= G132), Y336 (= Y133), G337 (= G134), L338 (≠ M135), T339 (= T136), D418 (= D214), K525 (= K320)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H37), F243 (≠ Y39), T247 (≠ H44), G335 (= G132), G337 (= G134), L338 (≠ M135), A344 (≠ V141)
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 96% coverage: 1:328/341 of query aligns to 174:499/506 of 4gxqA
- active site: N183 (= N10), H207 (= H37), T303 (= T136), E304 (= E137), I403 (≠ L235), N408 (= N240), A491 (≠ K320)
- binding adenosine-5'-triphosphate: H207 (= H37), S277 (≠ G110), A278 (≠ M111), P279 (≠ A112), E298 (= E131), M302 (= M135), T303 (= T136), D382 (= D214), R397 (= R229)
- binding carbonate ion: H207 (= H37), S277 (≠ G110), R299 (≠ G132), G301 (= G134)
Sites not aligning to the query:
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
34% identity, 96% coverage: 1:327/341 of query aligns to 193:526/530 of 5bsmA
- active site: S202 (≠ N10), H230 (= H37), T329 (= T136), E330 (= E137), K434 (≠ L235), Q439 (≠ N240), K519 (= K320)
- binding adenosine-5'-triphosphate: H230 (= H37), A302 (≠ G110), A303 (≠ M111), P304 (≠ A112), Y326 (= Y133), G327 (= G134), M328 (= M135), T329 (= T136), D413 (= D214), I425 (= I226), R428 (= R229), K519 (= K320)
Sites not aligning to the query:
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
34% identity, 96% coverage: 1:327/341 of query aligns to 192:525/528 of 5bsrA
- active site: S201 (≠ N10), H229 (= H37), T328 (= T136), E329 (= E137), K433 (≠ L235), Q438 (≠ N240), K518 (= K320)
- binding adenosine monophosphate: A301 (≠ G110), G326 (= G134), T328 (= T136), D412 (= D214), K429 (= K231), K433 (≠ L235), Q438 (≠ N240)
- binding coenzyme a: P226 (= P34), H229 (= H37), Y231 (= Y39), F253 (≠ R62), K435 (≠ S237), G436 (= G238), F437 (= F239), F498 (≠ G300)
Sites not aligning to the query:
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
34% identity, 96% coverage: 1:327/341 of query aligns to 193:526/529 of 5bsvA
- active site: S202 (≠ N10), H230 (= H37), T329 (= T136), E330 (= E137), K434 (≠ L235), Q439 (≠ N240), K519 (= K320)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H37), Y232 (= Y39), S236 (≠ F43), A302 (≠ G110), A303 (≠ M111), P304 (≠ A112), G325 (= G132), G327 (= G134), M328 (= M135), T329 (= T136), P333 (= P140), V334 (= V141), D413 (= D214), K430 (= K231), K434 (≠ L235), Q439 (≠ N240)
Sites not aligning to the query:
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
34% identity, 96% coverage: 1:327/341 of query aligns to 193:526/529 of 5bsuA
- active site: S202 (≠ N10), H230 (= H37), T329 (= T136), E330 (= E137), K434 (≠ L235), Q439 (≠ N240), K519 (= K320)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H37), Y232 (= Y39), S236 (≠ F43), M299 (≠ L107), A302 (≠ G110), A303 (≠ M111), P304 (≠ A112), G325 (= G132), G327 (= G134), M328 (= M135), T329 (= T136), P333 (= P140), D413 (= D214), K430 (= K231), K434 (≠ L235), Q439 (≠ N240)
Sites not aligning to the query:
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
34% identity, 96% coverage: 1:327/341 of query aligns to 193:526/529 of 5bstA
- active site: S202 (≠ N10), H230 (= H37), T329 (= T136), E330 (= E137), K434 (≠ L235), Q439 (≠ N240), K519 (= K320)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H37), Y232 (= Y39), S236 (≠ F43), A302 (≠ G110), A303 (≠ M111), P304 (≠ A112), G325 (= G132), Y326 (= Y133), G327 (= G134), M328 (= M135), T329 (= T136), P333 (= P140), V334 (= V141), D413 (= D214), K430 (= K231), K434 (≠ L235), Q439 (≠ N240)
Sites not aligning to the query:
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)
34% identity, 96% coverage: 1:327/341 of query aligns to 200:533/542 of O24146
- H237 (= H37) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y39) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ F43) binding ; binding ; binding
- K260 (≠ P61) binding
- A309 (≠ G110) binding ; binding ; binding
- Q331 (≠ E131) binding
- G332 (= G132) binding ; binding ; binding ; binding ; binding
- T336 (= T136) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V141) 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 (= D214) binding ; binding ; binding ; binding ; binding
- R435 (= R229) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K231) binding ; binding ; binding ; binding
- K441 (≠ L235) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S237) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G238) binding
- Q446 (≠ N240) binding
- K526 (= K320) binding ; mutation to A: Abolished activity against 4-coumarate.
Sites not aligning to the query:
- 189 binding
- 190 binding
- 191 binding
- 192 binding
- 193 binding ; T→A: Reduced activity against 4-coumarate.
- 197 binding ; K→A: Reduced 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)
31% identity, 96% coverage: 1:327/341 of query aligns to 214:547/556 of Q9S725
- M293 (≠ V80) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L107) mutation K->L,A: Affects the substrate specificity.
- E401 (= E181) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C183) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R229) mutation to Q: Drastically reduces the activity.
- K457 (≠ S237) mutation to S: Drastically reduces the activity.
- K540 (= K320) mutation to N: Abolishes the activity.
Sites not aligning to the query:
- 211 K→S: Drastically reduces the activity.
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)
32% identity, 96% coverage: 1:327/341 of query aligns to 231:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
6q2mA Crystal structure of photinus pyralis luciferase pps6 mutant in complex with dlsa (see paper)
30% identity, 96% coverage: 2:328/341 of query aligns to 209:536/544 of 6q2mA
- active site: R217 (≠ N10), H244 (= H37), T342 (= T136), E343 (= E137), K442 (≠ L235), Q447 (≠ N240), K528 (= K320)
- binding (2S,5S)-hexane-2,5-diol: R260 (≠ H54), Y279 (≠ W74)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H244 (= H37), F246 (≠ Y39), T250 (≠ H44), G315 (= G110), A316 (≠ M111), P317 (≠ A112), G338 (= G132), Y339 (= Y133), G340 (= G134), L341 (≠ M135), T342 (= T136), S346 (≠ P140), A347 (≠ V141), D421 (= D214), K528 (= K320)
Sites not aligning to the query:
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
33% identity, 96% coverage: 1:329/341 of query aligns to 193:528/528 of 3ni2A
- active site: S202 (≠ N10), H230 (= H37), T329 (= T136), E330 (= E137), K434 (≠ L235), Q439 (≠ N240), K519 (= K320)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y39), S236 (≠ F43), G302 (= G110), A303 (≠ M111), P304 (≠ A112), G325 (= G132), G327 (= G134), T329 (= T136), P333 (= P140), V334 (= V141), D413 (= D214), K430 (= K231), K434 (≠ L235), Q439 (≠ N240)
Sites not aligning to the query:
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
33% identity, 96% coverage: 1:329/341 of query aligns to 193:528/528 of 3a9vA
- active site: S202 (≠ N10), H230 (= H37), T329 (= T136), E330 (= E137), K434 (≠ L235), Q439 (≠ N240), K519 (= K320)
- binding adenosine monophosphate: H230 (= H37), G302 (= G110), A303 (≠ M111), P304 (≠ A112), Y326 (= Y133), G327 (= G134), M328 (= M135), T329 (= T136), D413 (= D214), K430 (= K231), K434 (≠ L235), Q439 (≠ N240)
Sites not aligning to the query:
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)
31% identity, 96% coverage: 1:327/341 of query aligns to 209:542/559 of Q67W82
- G395 (= G180) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
1ba3A Firefly luciferase in complex with bromoform (see paper)
30% identity, 96% coverage: 2:328/341 of query aligns to 206:533/540 of 1ba3A
- active site: R214 (≠ N10), H241 (= H37), T339 (= T136), E340 (= E137), K439 (≠ L235), Q444 (≠ N240), K525 (= K320)
- binding tribromomethane: E307 (≠ I105), G311 (= G109), R333 (≠ C130), R333 (≠ C130), T348 (≠ N145), E350 (≠ S147)
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_572 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_572
MLTHRNLVANMLQCKALMGSNLNEGCEILITPLPLYHIYAFTFHCMAMMLIGNHNILISN
PRDLTAMVKELSKWKFSGFVGLNTLFVALCNNEAFRKLDFSSLKITLSGGMALQLAAAER
WKEVAGCPICEGYGMTETSPVATVNPSQNIQIGTIGIPVPSTLCKVIDDAGVEQPLGAIG
ELCVKGPQVMKGYWQRQDATDEILDSEGWLKTGDIALIQPDGYMRIVDRKKDMILVSGFN
VYPNELEDVLATLPGVLQCAAIGVPDEKSGEAIKIFIVAKPGVTLTKDQVMEHMRANVTG
YKVPKAVEFRDALPTTNVGKILRRELRDEELKKLGVKKVSA
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