SitesBLAST
Comparing 3609708 FitnessBrowser__Dino:3609708 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, 93% coverage: 6:300/316 of query aligns to 2:285/291 of 3r7fA
- active site: R49 (= R58), T50 (= T59), K77 (= K86), R99 (= R108), H127 (= H136), Q130 (= Q139), L210 (= L222), P249 (= P263), G277 (= G292)
- binding phosphoric acid mono(formamide)ester: S47 (= S56), T48 (= T57), R49 (= R58), T50 (= T59), R99 (= R108), H127 (= H136), Q130 (= Q139), P249 (= P263), A250 (≠ G264)
- binding phosphate ion: S11 (≠ A15), T12 (≠ P16), Q23 (≠ D27), K26 (≠ R35), E140 (≠ R149), R171 (≠ K180), K241 (= K255), H243 (≠ D257), K272 (≠ E287), K272 (≠ E287), K275 (≠ E290)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 93% coverage: 6:300/316 of query aligns to 2:285/291 of 3r7dA
- active site: R49 (= R58), T50 (= T59), K77 (= K86), R99 (= R108), H127 (= H136), Q130 (= Q139), L210 (= L222), P249 (= P263), G277 (= G292)
- binding phosphate ion: S11 (≠ A15), T12 (≠ P16), T73 (≠ S82), S74 (= S83), K77 (= K86), R171 (≠ K180)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
41% identity, 93% coverage: 6:300/316 of query aligns to 2:285/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 93% coverage: 6:300/316 of query aligns to 2:285/290 of 3r7lA
- active site: R49 (= R58), T50 (= T59), K77 (= K86), R99 (= R108), H127 (= H136), Q130 (= Q139), L210 (= L222), P249 (= P263), G277 (= G292)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S56), T48 (= T57), R49 (= R58), T50 (= T59), S74 (= S83), K77 (= K86), R99 (= R108), H127 (= H136), R160 (= R169), R211 (= R223), Q213 (= Q225), A250 (≠ G264)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
40% identity, 95% coverage: 7:305/316 of query aligns to 3:293/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S56), T49 (= T57), R50 (= R58), T51 (= T59), S75 (= S83), K78 (= K86), R100 (= R108), H127 (= H136), R160 (= R169), R210 (= R223), Q212 (= Q225), A253 (≠ G264)
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)
41% identity, 80% coverage: 51:303/316 of query aligns to 40:289/291 of 4bjhB
- active site: R47 (= R58), T48 (= T59), K75 (= K86), R97 (= R108), H126 (= H136), Q129 (= Q139)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S56), T46 (= T57), R47 (= R58), T48 (= T59), R97 (= R108), H126 (= H136), R159 (= R169), V160 (= V170), R213 (= R223), Q215 (= Q225), G251 (= G264)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
41% identity, 80% coverage: 51:303/316 of query aligns to 40:289/291 of 3d6nB
- active site: R47 (= R58), T48 (= T59), K75 (= K86), R97 (= R108), H126 (= H136), Q129 (= Q139)
- binding citrate anion: T48 (= T59), R97 (= R108), H126 (= H136), R159 (= R169), V160 (= V170), R213 (= R223), G251 (= G264)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
35% identity, 94% coverage: 2:298/316 of query aligns to 2:298/307 of 5g1nE
- active site: R57 (= R58), T58 (= T59), K85 (= K86), R106 (= R108), H134 (= H136), Q137 (= Q139), T227 (≠ L222), P266 (= P263), G292 (= G292)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S56), T56 (= T57), R57 (= R58), T58 (= T59), S82 (= S83), K85 (= K86), R106 (= R108), H134 (= H136), R167 (= R169), R228 (= R223), Q230 (= Q225), M267 (≠ G264)
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)
35% identity, 95% coverage: 2:300/316 of query aligns to 1920:2218/2225 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
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, 95% coverage: 2:300/316 of query aligns to 1920:2218/2225 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.
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
33% identity, 93% coverage: 6:298/316 of query aligns to 3:283/292 of 5g1pA
- active site: R54 (= R58), T55 (= T59), K82 (= K86), R103 (= R108), H131 (= H136), Q134 (= Q139), T223 (≠ L222), P251 (= P263), G277 (= G292)
- binding phosphoric acid mono(formamide)ester: S52 (= S56), T53 (= T57), R54 (= R58), T55 (= T59), R103 (= R108), Q134 (= Q139), M252 (≠ G264)
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)
34% identity, 96% coverage: 2:303/316 of query aligns to 1919:2220/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
35% identity, 95% coverage: 6:306/316 of query aligns to 2:302/304 of 4eknB
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
35% identity, 83% coverage: 41:303/316 of query aligns to 50:314/316 of 8bplA
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
35% identity, 95% coverage: 3:303/316 of query aligns to 2:303/307 of 1ml4A
- active site: R56 (= R58), T57 (= T59), K85 (= K86), R106 (= R108), H134 (= H136), Q137 (= Q139), T227 (≠ L222), P266 (= P263), G292 (= G292)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S56), T55 (= T57), R56 (= R58), T57 (= T59), R106 (= R108), H134 (= H136), R167 (= R169), T168 (≠ V170), R228 (= R223), L267 (≠ G264)
P07259 Multifunctional protein URA2; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
35% identity, 95% coverage: 3:303/316 of query aligns to 1908:2209/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
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)
36% identity, 97% coverage: 2:306/316 of query aligns to 1914:2221/2224 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
P49077 Aspartate carbamoyltransferase, chloroplastic; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 85% coverage: 35:303/316 of query aligns to 113:386/390 of P49077
- R136 (= R58) binding
- T137 (= T59) binding
- R187 (= R108) binding
- H215 (= H136) binding
- R248 (= R169) binding
- R310 (= R223) binding
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
35% identity, 95% coverage: 3:303/316 of query aligns to 4:303/310 of 2ipoA
- active site: R54 (= R58), T55 (= T59), K84 (= K86), R105 (= R108), H134 (= H136), Q137 (= Q139), T228 (≠ L222), P266 (= P263), G292 (= G292)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S56), T53 (= T57), R54 (= R58), T55 (= T59), R105 (= R108), H134 (= H136), R167 (= R169), T168 (≠ V170), R229 (= R223), L267 (≠ G264)
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, 95% coverage: 3:303/316 of query aligns to 4:303/310 of 2h3eA
- active site: R54 (= R58), T55 (= T59), K84 (= K86), R105 (= R108), H134 (= H136), Q137 (= Q139), T228 (≠ L222), P266 (= P263), G292 (= G292)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S56), T53 (= T57), R54 (= R58), T55 (= T59), R105 (= R108), H134 (= H136), R167 (= R169), R229 (= R223), L267 (≠ G264)
Query Sequence
>3609708 FitnessBrowser__Dino:3609708
MTLRARHLLGIEHLAPDEIVTLLDLADRYADLNRRPDKHGDALDGLTQINMFFENSTRTQ
ASFEIAGKRLGADVMNMEVRASSIKKGETLIDTAMTLNAMHPDLLVVRHPHSGAVNLLAE
KVNCAVLNAGDGRHEHPTQALLDALTIRRAKGKLHRLNVAICGDIAHSRVARSNILLLGK
MENRIRLVGPRTLMPAEIAELGVEVYEDMKAGLDGVDVVMMLRLQKERMDGGFIPSEREY
YHRYGLDAEKLAYAKPDAIVMHPGPMNRGVEIDGTLADDINRSVIQEQVEMGVAVRMAAM
DLLARNLRAAREGVRA
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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