SitesBLAST
Comparing WP_041101383.1 NCBI__GCF_000828635.1:WP_041101383.1 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)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
39% identity, 94% coverage: 15:316/322 of query aligns to 1:285/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 94% coverage: 15:316/322 of query aligns to 1:285/290 of 3r7lA
- active site: R49 (= R68), T50 (= T69), K77 (= K96), R99 (= R118), H127 (= H152), Q130 (= Q155), L210 (= L239), P249 (= P280), G277 (= G308)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S66), T48 (= T67), R49 (= R68), T50 (= T69), S74 (= S93), K77 (= K96), R99 (= R118), H127 (= H152), R160 (= R185), R211 (= R240), Q213 (= Q242), A250 (≠ G281)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 94% coverage: 15:316/322 of query aligns to 1:285/291 of 3r7fA
- active site: R49 (= R68), T50 (= T69), K77 (= K96), R99 (= R118), H127 (= H152), Q130 (= Q155), L210 (= L239), P249 (= P280), G277 (= G308)
- binding phosphoric acid mono(formamide)ester: S47 (= S66), T48 (= T67), R49 (= R68), T50 (= T69), R99 (= R118), H127 (= H152), Q130 (= Q155), P249 (= P280), A250 (≠ G281)
- binding phosphate ion: S11 (≠ P25), T12 (≠ R26), Q23 (≠ A37), K26 (≠ R45), E140 (≠ H165), R171 (≠ T196), K241 (= K272), H243 (≠ D274), K272 (≠ P303), K272 (≠ P303), K275 (≠ T306)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 94% coverage: 15:316/322 of query aligns to 1:285/291 of 3r7dA
- active site: R49 (= R68), T50 (= T69), K77 (= K96), R99 (= R118), H127 (= H152), Q130 (= Q155), L210 (= L239), P249 (= P280), G277 (= G308)
- binding phosphate ion: S11 (≠ P25), T12 (≠ R26), T73 (≠ S92), S74 (= S93), K77 (= K96), R171 (≠ T196)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
37% identity, 95% coverage: 15:319/322 of query aligns to 1:291/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S66), T49 (= T67), R50 (= R68), T51 (= T69), S75 (= S93), K78 (= K96), R100 (= R118), H127 (= H152), R160 (= R185), R210 (= R240), Q212 (= Q242), A253 (≠ G281)
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)
38% identity, 95% coverage: 15:319/322 of query aligns to 1:289/291 of 4bjhB
- active site: R47 (= R68), T48 (= T69), K75 (= K96), R97 (= R118), H126 (= H152), Q129 (= Q155)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S66), T46 (= T67), R47 (= R68), T48 (= T69), R97 (= R118), H126 (= H152), R159 (= R185), V160 (= V186), R213 (= R240), Q215 (= Q242), G251 (= G281)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
38% identity, 95% coverage: 15:319/322 of query aligns to 1:289/291 of 3d6nB
- active site: R47 (= R68), T48 (= T69), K75 (= K96), R97 (= R118), H126 (= H152), Q129 (= Q155)
- binding citrate anion: T48 (= T69), R97 (= R118), H126 (= H152), R159 (= R185), V160 (= V186), R213 (= R240), G251 (= G281)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
34% identity, 95% coverage: 16:321/322 of query aligns to 6:305/307 of 5g1nE
- active site: R57 (= R68), T58 (= T69), K85 (= K96), R106 (= R118), H134 (= H152), Q137 (= Q155), T227 (≠ L239), P266 (= P280), G292 (= G308)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S66), T56 (= T67), R57 (= R68), T58 (= T69), S82 (= S93), K85 (= K96), R106 (= R118), H134 (= H152), R167 (= R185), R228 (= R240), Q230 (= Q242), M267 (≠ G281)
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)
34% identity, 95% coverage: 16:321/322 of query aligns to 1924:2223/2225 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: 16:321/322 of query aligns to 1924:2223/2225 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.
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
33% identity, 95% coverage: 16:321/322 of query aligns to 3:290/292 of 5g1pA
- active site: R54 (= R68), T55 (= T69), K82 (= K96), R103 (= R118), H131 (= H152), Q134 (= Q155), T223 (≠ L239), P251 (= P280), G277 (= G308)
- binding phosphoric acid mono(formamide)ester: S52 (= S66), T53 (= T67), R54 (= R68), T55 (= T69), R103 (= R118), Q134 (= Q155), M252 (≠ G281)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
34% identity, 95% coverage: 15:319/322 of query aligns to 1:299/304 of 4eknB
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
36% identity, 92% coverage: 26:321/322 of query aligns to 11:305/307 of 1ml4A
- active site: R56 (= R68), T57 (= T69), K85 (= K96), R106 (= R118), H134 (= H152), Q137 (= Q155), T227 (≠ L239), P266 (= P280), G292 (= G308)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S66), T55 (= T67), R56 (= R68), T57 (= T69), R106 (= R118), H134 (= H152), R167 (= R185), T168 (≠ V186), R228 (= R240), L267 (≠ G281)
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)
34% identity, 95% coverage: 16:321/322 of query aligns to 1918:2218/2224 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
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
34% identity, 83% coverage: 52:319/322 of query aligns to 51:314/316 of 8bplA
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)
31% identity, 95% coverage: 16:321/322 of query aligns to 1923:2222/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 94% coverage: 16:319/322 of query aligns to 8:304/311 of P0A786
- R55 (= R68) binding
- T56 (= T69) binding
- R106 (= R118) binding
- H135 (= H152) binding
- Q138 (= Q155) binding
- L268 (≠ G281) binding
- P269 (= P282) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
34% identity, 94% coverage: 16:319/322 of query aligns to 7:303/310 of 2hseA
- active site: R54 (= R68), T55 (= T69), K84 (= K96), R105 (= R118), H134 (= H152), Q137 (= Q155), T228 (≠ L239), P266 (= P280), G292 (= G308)
- binding aspartic acid: R54 (= R68), T55 (= T69), S58 (≠ T72), R105 (= R118), H134 (= H152), Q137 (= Q155), R167 (= R185), R229 (= R240), Q231 (= Q242), L267 (≠ G281), P268 (= P282), A289 (≠ V305), R296 (= R312)
- binding phosphonoacetamide: S52 (= S66), T53 (= T67), R54 (= R68), T55 (= T69), R105 (= R118), L267 (≠ G281)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
34% identity, 94% coverage: 16:319/322 of query aligns to 7:303/310 of 2a0fA
- active site: R54 (= R68), T55 (= T69), K84 (= K96), R105 (= R118), H134 (= H152), Q137 (= Q155), T228 (≠ L239), P266 (= P280), G292 (= G308)
- binding phosphonoacetamide: R54 (= R68), T55 (= T69), H134 (= H152), Q137 (= Q155), L267 (≠ G281)
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
33% identity, 94% coverage: 16:319/322 of query aligns to 7:303/310 of 2ipoA
- active site: R54 (= R68), T55 (= T69), K84 (= K96), R105 (= R118), H134 (= H152), Q137 (= Q155), T228 (≠ L239), P266 (= P280), G292 (= G308)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S66), T53 (= T67), R54 (= R68), T55 (= T69), R105 (= R118), H134 (= H152), R167 (= R185), T168 (≠ V186), R229 (= R240), L267 (≠ G281)
Query Sequence
>WP_041101383.1 NCBI__GCF_000828635.1:WP_041101383.1
MNTGGNPQLNSHGELQHLLTIEGLPRDVLTRILDTAAPFSEVAEREVKKVPLLRGKSVFN
LFFENSTRTRTTFEIAAKRLSADVINLNISTSSANKGETLLDTADNLAAMQADMFVVRHA
SSGAPYLIAQHLAATGRDHIHVVNAGDGRHAHPTQGLLDMYTIRHYKQDFSQLTIAIVGD
VLHSRVARSQIHALTTLGVPEVRVIAPKTLLPTGIERLGVRVFNDMREGLRGVDVVMMLR
LQNERMQGALLPSTQEYFKSWGLTPEKLQLAKPDAIVMHPGPMNRGVEIDSAVADGGQAV
ILPQVTFGIAVRMAVMAMLAGN
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