SitesBLAST
Comparing Pf1N1B4_575 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_575 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
52% identity, 99% coverage: 6:504/505 of query aligns to 5:495/561 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 (= E369) mutation to A: Loss of 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)
31% identity, 97% coverage: 16:503/505 of query aligns to 35:505/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 99% coverage: 5:504/505 of query aligns to 17:481/546 of Q84P21
Sites not aligning to the query:
- 530 K→N: Lossed enzymatic activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
30% identity, 91% coverage: 47:504/505 of query aligns to 43:470/528 of 3ni2A
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y271), S236 (≠ A275), G302 (= G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), G327 (= G366), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
Sites not aligning to the query:
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
30% identity, 91% coverage: 47:504/505 of query aligns to 43:470/528 of 3a9vA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473)
- binding adenosine monophosphate: H230 (= H269), G302 (= G342), A303 (≠ T343), P304 (≠ A344), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
Sites not aligning to the query:
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, 94% coverage: 29:504/505 of query aligns to 42:491/556 of Q9S725
- K211 (= K223) mutation to S: Drastically reduces the activity.
- M293 (≠ L312) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ N339) 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 (= R462) mutation to Q: Drastically reduces the activity.
- K457 (≠ S470) mutation to S: Drastically reduces the activity.
Sites not aligning to the query:
- 540 K→N: Abolishes the activity.
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
31% identity, 94% coverage: 28:504/505 of query aligns to 22:477/539 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 (= H269), F245 (= F273), T249 (≠ C277), G314 (= G342), A315 (≠ T343), P316 (≠ A344), G337 (= G364), Y338 (= Y365), G339 (= G366), L340 (= L367), T341 (= T368), S345 (≠ P372), A346 (≠ V373), D420 (= D447), I432 (= I459)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F273), R335 (= R360), G337 (= G364), G339 (= G366), L340 (= L367), A346 (≠ V373)
Sites not aligning to the query:
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
31% identity, 94% coverage: 28:504/505 of query aligns to 22:477/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H269), F245 (= F273), T249 (≠ C277), G314 (= G342), A315 (≠ T343), P316 (≠ A344), G337 (= G364), Y338 (= Y365), G339 (= G366), L340 (= L367), T341 (= T368), A346 (≠ V373), D420 (= D447), I432 (= I459)
Sites not aligning to the query:
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 93% coverage: 36:504/505 of query aligns to 29:469/528 of 5bsrA
- active site: S181 (≠ T215), S201 (≠ N235), H229 (= H269), T328 (= T368), E329 (= E369), K433 (≠ I468), Q438 (≠ N473)
- binding adenosine monophosphate: A301 (≠ G342), G326 (= G366), T328 (= T368), D412 (= D447), K429 (= K464), K433 (≠ I468), Q438 (≠ N473)
- binding coenzyme a: L102 (= L108), P226 (= P266), H229 (= H269), Y231 (= Y271), F253 (≠ R294), K435 (≠ S470), G436 (= G471), F437 (= F472)
Sites not aligning to the query:
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 93% coverage: 36:504/505 of query aligns to 30:470/530 of 5bsmA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473)
- binding adenosine-5'-triphosphate: S182 (≠ T215), S183 (≠ G216), G184 (= G217), T185 (= T218), T186 (= T219), K190 (= K223), H230 (= H269), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), D413 (= D447), I425 (= I459), R428 (= R462)
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)
30% identity, 93% coverage: 36:504/505 of query aligns to 37:477/542 of O24146
- S189 (≠ T215) binding
- S190 (≠ G216) binding
- G191 (= G217) binding
- T192 (= T218) binding
- T193 (= T219) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K223) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H269) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y271) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ A275) binding ; binding ; binding
- K260 (≠ P293) binding
- A309 (≠ G342) binding ; binding ; binding
- Q331 (≠ E363) binding
- G332 (= G364) binding ; binding ; binding ; binding ; binding
- T336 (= T368) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V373) 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 (= D447) binding ; binding ; binding ; binding ; binding
- R435 (= R462) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K464) binding ; binding ; binding ; binding
- K441 (≠ I468) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S470) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G471) binding
- Q446 (≠ N473) binding
Sites not aligning to the query:
- 526 binding ; K→A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 93% coverage: 36:504/505 of query aligns to 30:470/529 of 5bsvA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H269), Y232 (= Y271), S236 (≠ A275), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), G327 (= G366), M328 (≠ L367), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
Sites not aligning to the query:
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 93% coverage: 36:504/505 of query aligns to 30:470/529 of 5bsuA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H269), Y232 (= Y271), S236 (≠ A275), M299 (≠ N339), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), G327 (= G366), M328 (≠ L367), T329 (= T368), P333 (= P372), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
Sites not aligning to the query:
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 93% coverage: 36:504/505 of query aligns to 30:470/529 of 5bstA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H269), Y232 (= Y271), S236 (≠ A275), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 90% coverage: 47:498/505 of query aligns to 26:433/506 of 4gxqA
- active site: T163 (= T215), N183 (= N235), H207 (= H269), T303 (= T368), E304 (= E369), I403 (= I468), N408 (= N473)
- binding adenosine-5'-triphosphate: T163 (= T215), S164 (≠ G216), G165 (= G217), T166 (= T218), T167 (= T219), H207 (= H269), S277 (≠ G342), A278 (≠ T343), P279 (≠ A344), E298 (= E363), M302 (≠ L367), T303 (= T368), D382 (= D447), R397 (= R462)
- binding carbonate ion: H207 (= H269), S277 (≠ G342), R299 (≠ G364), G301 (= G366)
Sites not aligning to the query:
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
32% identity, 92% coverage: 42:504/505 of query aligns to 37:475/539 of 2d1sA
- active site: S194 (≠ T215), R214 (≠ N235), H241 (= H269), T339 (= T368), E340 (= E369), K439 (≠ I468), Q444 (≠ N473)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T215), S195 (≠ G216), H241 (= H269), F243 (≠ Y271), T247 (= T274), I282 (≠ L312), G312 (= G342), A313 (≠ T343), P314 (≠ A344), Q334 (≠ E363), G335 (= G364), Y336 (= Y365), G337 (= G366), L338 (= L367), T339 (= T368), S343 (≠ P372), A344 (≠ V373), D418 (= D447), R433 (= R462)
Sites not aligning to the query:
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
32% identity, 92% coverage: 42:504/505 of query aligns to 37:475/539 of 2d1rA
- active site: S194 (≠ T215), R214 (≠ N235), H241 (= H269), T339 (= T368), E340 (= E369), K439 (≠ I468), Q444 (≠ N473)
- binding adenosine monophosphate: S194 (≠ T215), S195 (≠ G216), H241 (= H269), G312 (= G342), A313 (≠ T343), P314 (≠ A344), G335 (= G364), Y336 (= Y365), G337 (= G366), L338 (= L367), T339 (= T368), D418 (= D447)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H269), F243 (≠ Y271), T247 (= T274), G335 (= G364), G337 (= G366), L338 (= L367), A344 (≠ V373)
Sites not aligning to the query:
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
30% identity, 91% coverage: 36:495/505 of query aligns to 29:460/527 of 5u95B
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)
28% identity, 97% coverage: 14:504/505 of query aligns to 28:486/559 of Q67W82
- G395 (= G413) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
6hpsA Near-infrared dual bioluminescence imaging in vivo using infra- luciferin (see paper)
30% identity, 94% coverage: 28:504/505 of query aligns to 20:475/539 of 6hpsA
- active site: S194 (≠ T215), R214 (≠ N235), H241 (= H269), T339 (= T368), E340 (= E369), K439 (≠ I468), Q444 (≠ N473)
- 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 (= H269), G242 (≠ I270), F243 (≠ Y271), S310 (= S340), G312 (= G342), A313 (≠ T343), P314 (≠ A344), R333 (= R360), G335 (= G364), Y336 (= Y365), G337 (= G366), L338 (= L367), T339 (= T368), A344 (≠ V373), D418 (= D447)
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_575 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_575
MQPDFWNDKRPAGVPLDIDLGAYKSVIEVFERSCKKFADRPAFSNMGVTLTYAELERYSA
AFAGYLQAHTDLMPGDRIAVQMPNVLHYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKD
SGARALVYLNVFGQKVQEVLPDTDIQYLIEAKMGDLMPTAKGWLVNTLVSKVKKMVPDYS
LPQAISFKSALRLGRGLGIKPLNVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMQQAR
ACLGQFGADGQPLLREGLEVMIAPLPLYHIYAFTANCMCMMVTGNHNVLITNPRDIGNFI
KELKNWRFSALLGLNTLFVALMDHPDFKTLDFSSLKLTNSGGTALVKATAERWEQLTGCR
ITEGYGLTETSPVACTNPYGDKSRIGTVGLPVPGTALKVINDEGVEQSLGERGELCIKGP
QIMKGYWQKPEATADVLDADGWFKSGDIAVIDPDGFVRIVDRKKDMIIVSGFNVYPNEIE
DVVMAHPKVANCAVIGVPDERSGRR
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