SitesBLAST
Comparing WP_086510656.1 NCBI__GCF_002151265.1:WP_086510656.1 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)
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)
44% identity, 92% coverage: 1:314/342 of query aligns to 1922:2222/2225 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.
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
44% identity, 91% coverage: 3:314/342 of query aligns to 6:304/307 of 5g1nE
- active site: R57 (= R54), T58 (= T55), K85 (= K83), R106 (= R104), H134 (= H132), Q137 (= Q135), T227 (= T230), P266 (= P271), G292 (= G302)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S52), T56 (= T53), R57 (= R54), T58 (= T55), S82 (= S80), K85 (= K83), R106 (= R104), H134 (= H132), R167 (= R169), R228 (= R231), Q230 (= Q233), M267 (≠ L272)
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)
44% identity, 92% coverage: 1:314/342 of query aligns to 1922:2222/2225 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
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
41% identity, 92% coverage: 3:318/342 of query aligns to 2:304/304 of 4eknB
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
43% identity, 91% coverage: 3:314/342 of query aligns to 3:289/292 of 5g1pA
- active site: R54 (= R54), T55 (= T55), K82 (= K83), R103 (= R104), H131 (= H132), Q134 (= Q135), T223 (= T230), P251 (= P271), G277 (= G302)
- binding phosphoric acid mono(formamide)ester: S52 (= S52), T53 (= T53), R54 (= R54), T55 (= T55), R103 (= R104), Q134 (= Q135), M252 (≠ L272)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
40% identity, 92% coverage: 3:316/342 of query aligns to 5:306/307 of 1ml4A
- active site: R56 (= R54), T57 (= T55), K85 (= K83), R106 (= R104), H134 (= H132), Q137 (= Q135), T227 (= T230), P266 (= P271), G292 (= G302)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S52), T55 (= T53), R56 (= R54), T57 (= T55), R106 (= R104), H134 (= H132), R167 (= R169), T168 (= T170), R228 (= R231), L267 (= L272)
6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
43% identity, 88% coverage: 13:314/342 of query aligns to 17:309/312 of 6ys6B
6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
43% identity, 88% coverage: 13:314/342 of query aligns to 17:309/312 of 6ypoA
- active site: R109 (= R104), H137 (= H132), Q140 (= Q135), T231 (= T230), P271 (= P271), G297 (= G302)
- binding uridine-5'-monophosphate: R58 (= R54), T59 (= T55), R109 (= R104), H137 (= H132), R170 (= R169), T171 (= T170), R232 (= R231), H270 (= H270), P271 (= P271), L272 (= L272)
6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate (see paper)
43% identity, 88% coverage: 13:314/342 of query aligns to 29:321/324 of 6yvbC
- active site: R121 (= R104), H149 (= H132), Q152 (= Q135), T243 (= T230), P283 (= P271), G309 (= G302)
- binding phosphoric acid mono(formamide)ester: S68 (= S52), T69 (= T53), R70 (= R54), T71 (= T55), R121 (= R104), H149 (= H132), Q152 (= Q135), P283 (= P271)
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)
40% identity, 90% coverage: 3:311/342 of query aligns to 1923:2218/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
P49077 Aspartate carbamoyltransferase, chloroplastic; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
43% identity, 88% coverage: 13:314/342 of query aligns to 95:387/390 of P49077
- R136 (= R54) binding
- T137 (= T55) binding
- R187 (= R104) binding
- H215 (= H132) binding
- R248 (= R169) binding
- R310 (= R231) binding
P05990 Multifunctional protein r; Protein rudimentary; 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 Drosophila melanogaster (Fruit fly) (see 2 papers)
40% identity, 92% coverage: 1:314/342 of query aligns to 1916:2217/2224 of P05990
Sites not aligning to the query:
- 1167 E→K: Severely diminishes UTP inhibition of CPSase; in Su(b).
- 1883 modified: Phosphoserine
- 1885 modified: Phosphoserine
- 1892 modified: Phosphoserine
- 1894 modified: Phosphoserine
2at1A Crystal structures of phosphonoacetamide ligated t and phosphonoacetamide and malonate ligated r states of aspartate carbamoyltransferase at 2.8-angstroms resolution and neutral ph (see paper)
39% identity, 92% coverage: 3:317/342 of query aligns to 7:307/310 of 2at1A
- active site: R54 (= R54), T55 (= T55), K84 (vs. gap), R105 (= R104), H134 (= H132), Q137 (= Q135), T228 (= T230), P266 (= P271), G292 (= G302)
- binding alpha-D-glucopyranose: R167 (= R169), R229 (= R231)
- binding phosphonoacetamide: S52 (= S52), T53 (= T53), R54 (= R54), T55 (= T55), R105 (= R104), H134 (= H132), Q137 (= Q135)
1at1A Crystal structures of phosphonoacetamide ligated t and phosphonoacetamide and malonate ligated r states of aspartate carbamoyltransferase at 2.8-angstroms resolution and neutral p H (see paper)
39% identity, 92% coverage: 3:317/342 of query aligns to 7:307/310 of 1at1A
- active site: R54 (= R54), T55 (= T55), K84 (vs. gap), R105 (= R104), H134 (= H132), Q137 (= Q135), T228 (= T230), P266 (= P271), G292 (= G302)
- binding malonate ion: H134 (= H132), R167 (= R169), R229 (= R231), Q231 (= Q233)
- binding phosphonoacetamide: S52 (= S52), T53 (= T53), R54 (= R54), T55 (= T55), R105 (= R104), H134 (= H132), Q137 (= Q135)
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
39% identity, 92% coverage: 3:317/342 of query aligns to 7:307/310 of 2hseA
- active site: R54 (= R54), T55 (= T55), K84 (vs. gap), R105 (= R104), H134 (= H132), Q137 (= Q135), T228 (= T230), P266 (= P271), G292 (= G302)
- binding aspartic acid: R54 (= R54), T55 (= T55), S58 (= S58), R105 (= R104), H134 (= H132), Q137 (= Q135), R167 (= R169), R229 (= R231), Q231 (= Q233), L267 (= L272), P268 (= P273), A289 (≠ T299), R296 (= R306)
- binding phosphonoacetamide: S52 (= S52), T53 (= T53), R54 (= R54), T55 (= T55), R105 (= R104), L267 (= L272)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
39% identity, 92% coverage: 3:317/342 of query aligns to 7:307/310 of 2a0fA
- active site: R54 (= R54), T55 (= T55), K84 (vs. gap), R105 (= R104), H134 (= H132), Q137 (= Q135), T228 (= T230), P266 (= P271), G292 (= G302)
- binding phosphonoacetamide: R54 (= R54), T55 (= T55), H134 (= H132), Q137 (= Q135), L267 (= L272)
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
39% identity, 92% coverage: 3:317/342 of query aligns to 8:308/311 of P0A786
- R55 (= R54) binding
- T56 (= T55) binding
- R106 (= R104) binding
- H135 (= H132) binding
- Q138 (= Q135) binding
- L268 (= L272) binding
- P269 (= P273) 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)
39% identity, 92% coverage: 3:317/342 of query aligns to 7:307/310 of 2ipoA
- active site: R54 (= R54), T55 (= T55), K84 (vs. gap), R105 (= R104), H134 (= H132), Q137 (= Q135), T228 (= T230), P266 (= P271), G292 (= G302)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S52), T53 (= T53), R54 (= R54), T55 (= T55), R105 (= R104), H134 (= H132), R167 (= R169), T168 (= T170), R229 (= R231), L267 (= L272)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
39% identity, 92% coverage: 3:317/342 of query aligns to 7:307/310 of 2h3eA
- active site: R54 (= R54), T55 (= T55), K84 (vs. gap), R105 (= R104), H134 (= H132), Q137 (= Q135), T228 (= T230), P266 (= P271), G292 (= G302)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S52), T53 (= T53), R54 (= R54), T55 (= T55), R105 (= R104), H134 (= H132), R167 (= R169), R229 (= R231), L267 (= L272)
2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
39% identity, 92% coverage: 3:317/342 of query aligns to 7:307/310 of 2fzkA
- active site: R54 (= R54), T55 (= T55), K84 (vs. gap), R105 (= R104), H134 (= H132), Q137 (= Q135), T228 (= T230), P266 (= P271), G292 (= G302)
- binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T55), H134 (= H132), Q137 (= Q135), T168 (= T170), R229 (= R231), P266 (= P271), L267 (= L272), R296 (= R306)
Query Sequence
>WP_086510656.1 NCBI__GCF_002151265.1:WP_086510656.1
MSRHLLSVDSLTRDSVNHLMHVAARMEPIAQRRQVTRVLEGAVLGNLFFEASTRTRVSFH
TAFCRLGGSVCDTTGFTFSSMAKGESLYDTSRVMSGYCDAIVMRHPDQGSVAEFAAATHV
PVINGGDGPGEHPSQALLDFYTIDKEFTRLGKKLAGAHVLLTGDLKYGRTVHSLIKLLSL
YDPMRITLVAPPGLEMPDYLIDLVASRGHRIEQRTSLADDYADVDVVYTTRIQKERFTAE
MSEGFSLSRDFTVDRAFMDKRCGRDTIVMHPLPRDSRPEANDLDVDLNGDPRLAIFRQTD
NGIPVRMAIFATLLQVDELIEKDLRPVRWFVPERVGVDDSAL
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