SitesBLAST
Comparing WP_084275302.1 NCBI__GCF_900176045.1:WP_084275302.1 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)
38% identity, 99% coverage: 3:290/291 of query aligns to 2:290/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
38% identity, 99% coverage: 3:290/291 of query aligns to 2:290/290 of 3r7lA
- active site: R49 (= R50), T50 (= T51), K77 (= K78), R99 (= R100), H127 (= H128), Q130 (= Q131), L210 (= L210), P249 (= P249), G277 (= G277)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S48), T48 (= T49), R49 (= R50), T50 (= T51), S74 (= S75), K77 (= K78), R99 (= R100), H127 (= H128), R160 (= R161), R211 (= R211), Q213 (= Q213), A250 (≠ G250)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
38% identity, 99% coverage: 3:290/291 of query aligns to 2:290/291 of 3r7fA
- active site: R49 (= R50), T50 (= T51), K77 (= K78), R99 (= R100), H127 (= H128), Q130 (= Q131), L210 (= L210), P249 (= P249), G277 (= G277)
- binding phosphoric acid mono(formamide)ester: S47 (= S48), T48 (= T49), R49 (= R50), T50 (= T51), R99 (= R100), H127 (= H128), Q130 (= Q131), P249 (= P249), A250 (≠ G250)
- binding phosphate ion: S11 (≠ K12), T12 (≠ K13), Q23 (≠ T24), K26 (≠ L27), E140 (≠ Q141), R171 (= R172), K241 (≠ D241), H243 (≠ D243), K272 (≠ E272), K272 (≠ E272), K275 (≠ R275)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
38% identity, 99% coverage: 3:290/291 of query aligns to 2:290/291 of 3r7dA
- active site: R49 (= R50), T50 (= T51), K77 (= K78), R99 (= R100), H127 (= H128), Q130 (= Q131), L210 (= L210), P249 (= P249), G277 (= G277)
- binding phosphate ion: S11 (≠ K12), T12 (≠ K13), T73 (≠ S74), S74 (= S75), K77 (= K78), R171 (= R172)
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)
36% identity, 97% coverage: 3:284/291 of query aligns to 2:285/291 of 4bjhB
- active site: R47 (= R50), T48 (= T51), K75 (= K78), R97 (= R100), H126 (= H128), Q129 (= Q131)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S48), T46 (= T49), R47 (= R50), T48 (= T51), R97 (= R100), H126 (= H128), R159 (= R161), V160 (= V162), R213 (= R211), Q215 (= Q213), G251 (= G250)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
36% identity, 97% coverage: 3:284/291 of query aligns to 2:285/291 of 3d6nB
- active site: R47 (= R50), T48 (= T51), K75 (= K78), R97 (= R100), H126 (= H128), Q129 (= Q131)
- binding citrate anion: T48 (= T51), R97 (= R100), H126 (= H128), R159 (= R161), V160 (= V162), R213 (= R211), G251 (= G250)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
33% identity, 98% coverage: 4:289/291 of query aligns to 3:292/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S48), T49 (= T49), R50 (= R50), T51 (= T51), S75 (= S75), K78 (= K78), R100 (= R100), H127 (= H128), R160 (= R161), R210 (= R211), Q212 (= Q213), A253 (≠ G250)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
33% identity, 99% coverage: 3:289/291 of query aligns to 6:304/307 of 5g1nE
- active site: R57 (= R50), T58 (= T51), K85 (= K78), R106 (= R100), H134 (= H128), Q137 (= Q131), T227 (≠ L210), P266 (= P249), G292 (= G277)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S48), T56 (= T49), R57 (= R50), T58 (= T51), S82 (= S75), K85 (= K78), R106 (= R100), H134 (= H128), R167 (= R161), R228 (= R211), Q230 (= Q213), M267 (≠ G250)
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)
33% identity, 99% coverage: 1:289/291 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.
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, 99% coverage: 1:289/291 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
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
33% identity, 99% coverage: 3:289/291 of query aligns to 3:289/292 of 5g1pA
- active site: R54 (= R50), T55 (= T51), K82 (= K78), R103 (= R100), H131 (= H128), Q134 (= Q131), T223 (≠ L210), P251 (= P249), G277 (= G277)
- binding phosphoric acid mono(formamide)ester: S52 (= S48), T53 (= T49), R54 (= R50), T55 (= T51), R103 (= R100), Q134 (= Q131), M252 (≠ G250)
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, 100% coverage: 1:291/291 of query aligns to 1916:2219/2224 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 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)
34% identity, 99% coverage: 3:289/291 of query aligns to 1911:2210/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
34% identity, 99% coverage: 3:290/291 of query aligns to 2:301/304 of 4eknB
6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate (see paper)
35% identity, 99% coverage: 5:291/291 of query aligns to 21:323/324 of 6yvbC
- active site: R121 (= R100), H149 (= H128), Q152 (= Q131), T243 (≠ L210), P283 (= P249), G309 (= G277)
- binding phosphoric acid mono(formamide)ester: S68 (= S48), T69 (= T49), R70 (= R50), T71 (= T51), R121 (= R100), H149 (= H128), Q152 (= Q131), P283 (= P249)
6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
35% identity, 99% coverage: 5:291/291 of query aligns to 9:311/312 of 6ys6B
6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
35% identity, 99% coverage: 5:291/291 of query aligns to 9:311/312 of 6ypoA
- active site: R109 (= R100), H137 (= H128), Q140 (= Q131), T231 (≠ L210), P271 (= P249), G297 (= G277)
- binding uridine-5'-monophosphate: R58 (= R50), T59 (= T51), R109 (= R100), H137 (= H128), R170 (= R161), T171 (≠ V162), R232 (= R211), H270 (= H248), P271 (= P249), L272 (≠ G250)
P49077 Aspartate carbamoyltransferase, chloroplastic; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 99% coverage: 5:291/291 of query aligns to 87:389/390 of P49077
- R136 (= R50) binding
- T137 (= T51) binding
- R187 (= R100) binding
- H215 (= H128) binding
- R248 (= R161) binding
- R310 (= R211) binding
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, 99% coverage: 3:291/291 of query aligns to 1923:2222/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
36% identity, 98% coverage: 2:285/291 of query aligns to 4:300/307 of 1ml4A
- active site: R56 (= R50), T57 (= T51), K85 (= K78), R106 (= R100), H134 (= H128), Q137 (= Q131), T227 (≠ L210), P266 (= P249), G292 (= G277)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S48), T55 (= T49), R56 (= R50), T57 (= T51), R106 (= R100), H134 (= H128), R167 (= R161), T168 (≠ V162), R228 (= R211), L267 (≠ G250)
Query Sequence
>WP_084275302.1 NCBI__GCF_900176045.1:WP_084275302.1
MSKHLITTKDLKKEEIEDIFNLATQFLQPPYEKLLQDKLIITIFFENSTRTRSSFEVAAK
NLGAQVVNLDVTRSSTKKGETLFDTAANLDAMGPNAIVVRHKHAGAPALLARHVSCSLIN
GGDGAHAHPTQALLDLFTLKQHLGNVQGKKIAIVGDIKNSRVANSNIELLTRFGMEVILV
APPHFLPPTSLRTSSSLQEVIDEVDAIMSLRTQTERHKYPIYASLRDYGSDFCITKDLIG
DRDILILHPGPVHRNIDISDEVLADPRCKVLEQVRNGVVVRMAILVKLIHG
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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