SitesBLAST
Comparing GFF294 FitnessBrowser__Phaeo:GFF294 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)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 89% coverage: 16:310/331 of query aligns to 2:285/291 of 3r7fA
- active site: R49 (= R68), T50 (= T69), K77 (= K96), R99 (= R118), H127 (= H146), Q130 (= Q149), L210 (= L232), P249 (= P273), G277 (= G302)
- binding phosphoric acid mono(formamide)ester: S47 (= S66), T48 (= T67), R49 (= R68), T50 (= T69), R99 (= R118), H127 (= H146), Q130 (= Q149), P249 (= P273), A250 (≠ G274)
- binding phosphate ion: S11 (≠ K25), T12 (≠ P26), Q23 (≠ A40), K26 (≠ R45), E140 (≠ R159), R171 (≠ K190), K241 (= K265), H243 (≠ D267), K272 (≠ E297), K272 (≠ E297), K275 (≠ E300)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 89% coverage: 16:310/331 of query aligns to 2:285/291 of 3r7dA
- active site: R49 (= R68), T50 (= T69), K77 (= K96), R99 (= R118), H127 (= H146), Q130 (= Q149), L210 (= L232), P249 (= P273), G277 (= G302)
- binding phosphate ion: S11 (≠ K25), T12 (≠ P26), T73 (≠ S92), S74 (= S93), K77 (= K96), R171 (≠ K190)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 89% coverage: 16:310/331 of query aligns to 2:285/290 of 3r7lA
- active site: R49 (= R68), T50 (= T69), K77 (= K96), R99 (= R118), H127 (= H146), Q130 (= Q149), L210 (= L232), P249 (= P273), G277 (= G302)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S66), T48 (= T67), R49 (= R68), T50 (= T69), S74 (= S93), K77 (= K96), R99 (= R118), H127 (= H146), R160 (= R179), R211 (= R233), Q213 (= Q235), A250 (≠ G274)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
41% identity, 89% coverage: 16:310/331 of query aligns to 2:285/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
38% identity, 90% coverage: 17:315/331 of query aligns to 3:293/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S66), T49 (= T67), R50 (= R68), T51 (= T69), S75 (= S93), K78 (= K96), R100 (= R118), H127 (= H146), R160 (= R179), R210 (= R233), Q212 (= Q235), A253 (≠ G274)
4bjhB Crystal structure of the aquifex reactor complex formed by dihydroorotase (h180a, h232a) with dihydroorotate and aspartate transcarbamoylase with n-(phosphonacetyl)-l-aspartate (pala) (see paper)
37% identity, 90% coverage: 16:313/331 of query aligns to 2:289/291 of 4bjhB
- active site: R47 (= R68), T48 (= T69), K75 (= K96), R97 (= R118), H126 (= H146), Q129 (= Q149)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S66), T46 (= T67), R47 (= R68), T48 (= T69), R97 (= R118), H126 (= H146), R159 (= R179), V160 (= V180), R213 (= R233), Q215 (= Q235), G251 (= G274)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
37% identity, 90% coverage: 16:313/331 of query aligns to 2:289/291 of 3d6nB
- active site: R47 (= R68), T48 (= T69), K75 (= K96), R97 (= R118), H126 (= H146), Q129 (= Q149)
- binding citrate anion: T48 (= T69), R97 (= R118), H126 (= H146), R159 (= R179), V160 (= V180), R213 (= R233), G251 (= G274)
P08955 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
34% identity, 92% coverage: 6:310/331 of query aligns to 1914:2218/2225 of P08955
Sites not aligning to the query:
- 1406 modified: Phosphoserine; by PKA; S→A: No effect on enzyme kinetics.; S→D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.
P27708 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
33% identity, 92% coverage: 6:310/331 of query aligns to 1914:2218/2225 of P27708
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 33 M → R: in DEE50; uncertain significance; dbSNP:rs751610198
- 177 R → Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292
- 456 modified: Phosphothreonine; by MAPK1
- 735 Y → C: in a colorectal cancer sample; somatic mutation
- 1406 modified: Phosphoserine; by PKA
- 1471 binding ; binding ; H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
- 1473 binding ; H→A: No zinc-binding and no catalytic activity.
- 1475 binding
- 1505 binding
- 1512 D→N: No change in catalytic activity.
- 1556 binding via carbamate group; binding via carbamate group; modified: N6-carboxylysine
- 1562 T→A: Abolishes dihydroorotase activity.
- 1563 F→A: Abolishes dihydroorotase activity.
- 1590 binding ; H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
- 1613 binding ; C→S: Reduces dihydroorotase activity.
- 1614 binding ; H→A: Abolishes dihydroorotase activity.
- 1637 binding ; E→T: Abolishes dihydroorotase activity.
- 1642 H→N: 11.5% of wild-type catalytic activity.
- 1661 binding
- 1686 binding ; D→N: Abolishes dihydroorotase activity.
- 1690 binding ; H→N: 3% of wild-type catalytic activity.
- 1702 binding
- 1789:2225 natural variant: Missing (in DEE50; uncertain significance)
- 1859 modified: Phosphoserine; by RPS6KB1 and PKA
- 1873 modified: Phosphoserine; by PKC; in vitro; S→A: Abolishes PMA-induced Thr-456 phosphorylation.
- 1900 modified: Phosphoserine
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
34% identity, 89% coverage: 16:308/331 of query aligns to 6:298/307 of 5g1nE
- active site: R57 (= R68), T58 (= T69), K85 (= K96), R106 (= R118), H134 (= H146), Q137 (= Q149), T227 (≠ L232), P266 (= P273), G292 (= G302)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S66), T56 (= T67), R57 (= R68), T58 (= T69), S82 (= S93), K85 (= K96), R106 (= R118), H134 (= H146), R167 (= R179), R228 (= R233), Q230 (= Q235), M267 (≠ G274)
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
33% identity, 89% coverage: 16:308/331 of query aligns to 3:283/292 of 5g1pA
- active site: R54 (= R68), T55 (= T69), K82 (= K96), R103 (= R118), H131 (= H146), Q134 (= Q149), T223 (≠ L232), P251 (= P273), G277 (= G302)
- binding phosphoric acid mono(formamide)ester: S52 (= S66), T53 (= T67), R54 (= R68), T55 (= T69), R103 (= R118), Q134 (= Q149), M252 (≠ G274)
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
33% identity, 92% coverage: 10:313/331 of query aligns to 10:314/316 of 8bplA
P49077 Aspartate carbamoyltransferase, chloroplastic; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 86% coverage: 29:313/331 of query aligns to 98:386/390 of P49077
- R136 (= R68) binding
- T137 (= T69) binding
- R187 (= R118) binding
- H215 (= H146) binding
- R248 (= R179) binding
- R310 (= R233) binding
6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
35% identity, 86% coverage: 29:313/331 of query aligns to 20:308/312 of 6ys6B
6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
35% identity, 86% coverage: 29:313/331 of query aligns to 20:308/312 of 6ypoA
- active site: R109 (= R118), H137 (= H146), Q140 (= Q149), T231 (≠ L232), P271 (= P273), G297 (= G302)
- binding uridine-5'-monophosphate: R58 (= R68), T59 (= T69), R109 (= R118), H137 (= H146), R170 (= R179), T171 (≠ V180), R232 (= R233), H270 (= H272), P271 (= P273), L272 (≠ G274)
P20054 Multifunctional protein pyr1-3; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Dictyostelium discoideum (Social amoeba)
32% identity, 91% coverage: 12:313/331 of query aligns to 1919:2220/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate (see paper)
35% identity, 86% coverage: 29:313/331 of query aligns to 32:320/324 of 6yvbC
- active site: R121 (= R118), H149 (= H146), Q152 (= Q149), T243 (≠ L232), P283 (= P273), G309 (= G302)
- binding phosphoric acid mono(formamide)ester: S68 (= S66), T69 (= T67), R70 (= R68), T71 (= T69), R121 (= R118), H149 (= H146), Q152 (= Q149), P283 (= P273)
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
35% identity, 92% coverage: 15:317/331 of query aligns to 7:309/311 of P0A786
- R55 (= R68) binding
- T56 (= T69) binding
- R106 (= R118) binding
- H135 (= H146) binding
- Q138 (= Q149) binding
- L268 (≠ G274) binding
- P269 (= P275) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
35% identity, 92% coverage: 15:317/331 of query aligns to 6:308/310 of 2ipoA
- active site: R54 (= R68), T55 (= T69), K84 (= K96), R105 (= R118), H134 (= H146), Q137 (= Q149), T228 (≠ L232), P266 (= P273), G292 (= G302)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S66), T53 (= T67), R54 (= R68), T55 (= T69), R105 (= R118), H134 (= H146), R167 (= R179), T168 (≠ V180), R229 (= R233), L267 (≠ G274)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
35% identity, 92% coverage: 15:317/331 of query aligns to 6:308/310 of 2h3eA
- active site: R54 (= R68), T55 (= T69), K84 (= K96), R105 (= R118), H134 (= H146), Q137 (= Q149), T228 (≠ L232), P266 (= P273), G292 (= G302)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S66), T53 (= T67), R54 (= R68), T55 (= T69), R105 (= R118), H134 (= H146), R167 (= R179), R229 (= R233), L267 (≠ G274)
Query Sequence
>GFF294 FitnessBrowser__Phaeo:GFF294
MPTATSSPDPMAFSQRHLLGIEPLKPHEITAILDLADSYAELNRRPDKHANALSGLTQVN
MFFENSTRTQASFEIAGKRLGADVMNMAMQASSIKKGETLIDTAMTLNAMHPDLLVVRHP
HSGAVDLLAQKVNCAVLNAGDGRHEHPTQALLDALTIRRAKGRLHRLNIAICGDVAHSRV
ARSNLILLGKMENRIRLIGPPTLVPGHFADFGAEIYDDMREGLKDVDVVMMLRLQKERMD
GGFIPSEREYYHRYGLDAEKLALAKPDAIVMHPGPMNRGVEIDGTLADDINRSVIQEQVE
MGVAVRMAAMDLLARNLRASRERAASQPGVA
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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