SitesBLAST
Comparing 5208502 FitnessBrowser__PV4:5208502 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)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
43% identity, 93% coverage: 4:319/339 of query aligns to 2:306/307 of 1ml4A
- active site: R56 (= R58), T57 (= T59), K85 (= K87), R106 (= R108), H134 (= H136), Q137 (= Q139), T227 (= T234), P266 (= P274), G292 (= G305)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S56), T55 (= T57), R56 (= R58), T57 (= T59), R106 (= R108), H134 (= H136), Q137 (= Q139), R167 (= R173), T168 (= T174), R228 (= R235), Q230 (= Q237), P266 (= P274), L267 (= L275), P268 (= P276)
P08955 CAD protein; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
45% identity, 92% coverage: 6:318/339 of query aligns to 1923:2223/2225 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, 92% coverage: 6:318/339 of query aligns to 5:305/307 of 5g1nE
- active site: R57 (= R58), T58 (= T59), K85 (= K87), R106 (= R108), H134 (= H136), Q137 (= Q139), T227 (= T234), P266 (= P274), G292 (= G305)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S56), T56 (= T57), R57 (= R58), T58 (= T59), S82 (= S84), K85 (= K87), R106 (= R108), H134 (= H136), R167 (= R173), T168 (= T174), R228 (= R235), Q230 (= Q237), P266 (= P274), M267 (≠ L275)
P27708 CAD protein; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
44% identity, 92% coverage: 6:318/339 of query aligns to 1923:2223/2225 of P27708
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 33 M → R: in DEE50; unknown pathological 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 ; binding ; D→N: Abolishes dihydroorotase activity.
- 1690 binding ; H→N: 3% of wild-type catalytic activity.
- 1789:2225 natural variant: Missing (in DEE50; unknown pathological 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
P20054 Protein PYR1-3; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Dictyostelium discoideum (Social amoeba)
43% identity, 92% coverage: 6:318/339 of query aligns to 1922:2222/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
Q09794 Protein ura1; EC 6.3.5.5; EC 2.1.3.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
44% identity, 94% coverage: 2:318/339 of query aligns to 1932:2238/2244 of Q09794
Sites not aligning to the query:
- 1119 modified: Phosphoserine
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
P05990 CAD protein; Protein rudimentary; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Drosophila melanogaster (Fruit fly) (see 2 papers)
43% identity, 93% coverage: 4:318/339 of query aligns to 1915:2218/2224 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
P07259 Protein URA2; EC 6.3.5.5; EC 2.1.3.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
42% identity, 94% coverage: 4:320/339 of query aligns to 1908:2213/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
3e2pA Catalytic subunit of m. Jannaschii aspartate transcarbamoylase in an orthorhombic crystal form (see paper)
42% identity, 91% coverage: 7:313/339 of query aligns to 2:296/306 of 3e2pA
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
43% identity, 92% coverage: 6:318/339 of query aligns to 2:290/292 of 5g1pA
- active site: R54 (= R58), T55 (= T59), K82 (= K87), R103 (= R108), H131 (= H136), Q134 (= Q139), T223 (= T234), P251 (= P274), G277 (= G305)
- binding phosphoric acid mono(formamide)ester: S52 (= S56), T53 (= T57), R54 (= R58), T55 (= T59), R103 (= R108), H131 (= H136), Q134 (= Q139), P251 (= P274), M252 (≠ L275)
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
43% identity, 93% coverage: 2:317/339 of query aligns to 11:315/316 of 8bplA
6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate (see paper)
41% identity, 93% coverage: 4:317/339 of query aligns to 10:321/324 of 6yvbC
- active site: R121 (= R108), H149 (= H136), Q152 (= Q139), T243 (= T234), P283 (= P274), G309 (= G305)
- binding phosphoric acid mono(formamide)ester: S68 (= S56), T69 (= T57), R70 (= R58), T71 (= T59), R121 (= R108), H149 (= H136), Q152 (= Q139), P283 (= P274), L284 (= L275)
6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
41% identity, 93% coverage: 4:317/339 of query aligns to 4:309/312 of 6ys6B
6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
41% identity, 93% coverage: 4:317/339 of query aligns to 4:309/312 of 6ypoA