SitesBLAST
Comparing 8500677 FitnessBrowser__Miya:8500677 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)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
40% identity, 90% coverage: 14:306/325 of query aligns to 4:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S62), T49 (= T63), R50 (= R64), T51 (= T65), S75 (= S89), K78 (= K92), R100 (= R114), H127 (= H142), R160 (= R176), R210 (= R230), Q212 (= Q232), A253 (≠ G271)
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, 92% coverage: 12:311/325 of query aligns to 2:291/291 of 4bjhB
- active site: R47 (= R64), T48 (= T65), K75 (= K92), R97 (= R114), H126 (= H142), Q129 (= Q145)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S62), T46 (= T63), R47 (= R64), T48 (= T65), R97 (= R114), H126 (= H142), R159 (= R176), V160 (= V177), R213 (= R230), Q215 (= Q232), G251 (= G271)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
36% identity, 92% coverage: 12:311/325 of query aligns to 2:291/291 of 3d6nB
- active site: R47 (= R64), T48 (= T65), K75 (= K92), R97 (= R114), H126 (= H142), Q129 (= Q145)
- binding citrate anion: T48 (= T65), R97 (= R114), H126 (= H142), R159 (= R176), V160 (= V177), R213 (= R230), G251 (= G271)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
36% identity, 91% coverage: 12:306/325 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)
36% identity, 91% coverage: 12:306/325 of query aligns to 2:285/290 of 3r7lA
- active site: R49 (= R64), T50 (= T65), K77 (= K92), R99 (= R114), H127 (= H142), Q130 (= Q145), L210 (= L229), P249 (= P270), G277 (= G298)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S62), T48 (= T63), R49 (= R64), T50 (= T65), S74 (= S89), K77 (= K92), R99 (= R114), H127 (= H142), R160 (= R176), R211 (= R230), Q213 (= Q232), A250 (≠ G271)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
36% identity, 91% coverage: 12:306/325 of query aligns to 2:285/291 of 3r7fA
- active site: R49 (= R64), T50 (= T65), K77 (= K92), R99 (= R114), H127 (= H142), Q130 (= Q145), L210 (= L229), P249 (= P270), G277 (= G298)
- binding phosphoric acid mono(formamide)ester: S47 (= S62), T48 (= T63), R49 (= R64), T50 (= T65), R99 (= R114), H127 (= H142), Q130 (= Q145), P249 (= P270), A250 (≠ G271)
- binding phosphate ion: S11 (≠ T21), T12 (≠ R22), Q23 (≠ A33), K26 (≠ R41), E140 (≠ Q155), R171 (≠ S187), K241 (≠ A262), H243 (≠ S264), K272 (≠ D293), K272 (≠ D293), K275 (≠ A296)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
36% identity, 91% coverage: 12:306/325 of query aligns to 2:285/291 of 3r7dA
- active site: R49 (= R64), T50 (= T65), K77 (= K92), R99 (= R114), H127 (= H142), Q130 (= Q145), L210 (= L229), P249 (= P270), G277 (= G298)
- binding phosphate ion: S11 (≠ T21), T12 (≠ R22), T73 (≠ S88), S74 (= S89), K77 (= K92), R171 (≠ S187)
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
33% identity, 91% coverage: 12:306/325 of query aligns to 3:285/292 of 5g1pA
- active site: R54 (= R64), T55 (= T65), K82 (= K92), R103 (= R114), H131 (= H142), Q134 (= Q145), T223 (≠ L229), P251 (= P270), G277 (= G298)
- binding phosphoric acid mono(formamide)ester: S52 (= S62), T53 (= T63), R54 (= R64), T55 (= T65), R103 (= R114), Q134 (= Q145), M252 (≠ G271)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
33% identity, 91% coverage: 12:306/325 of query aligns to 6:300/307 of 5g1nE
- active site: R57 (= R64), T58 (= T65), K85 (= K92), R106 (= R114), H134 (= H142), Q137 (= Q145), T227 (≠ L229), P266 (= P270), G292 (= G298)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S62), T56 (= T63), R57 (= R64), T58 (= T65), S82 (= S89), K85 (= K92), R106 (= R114), H134 (= H142), R167 (= R176), R228 (= R230), Q230 (= Q232), M267 (≠ G271)
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, 91% coverage: 12:306/325 of query aligns to 1924:2218/2225 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.
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
33% identity, 93% coverage: 9:309/325 of query aligns to 2:303/307 of 1ml4A
- active site: R56 (= R64), T57 (= T65), K85 (= K92), R106 (= R114), H134 (= H142), Q137 (= Q145), T227 (≠ L229), P266 (= P270), G292 (= G298)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S62), T55 (= T63), R56 (= R64), T57 (= T65), R106 (= R114), H134 (= H142), R167 (= R176), T168 (≠ V177), R228 (= R230), L267 (≠ G271)
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, 91% coverage: 12:306/325 of query aligns to 1924:2218/2225 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
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
34% identity, 94% coverage: 8:311/325 of query aligns to 12:316/316 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, 92% coverage: 12:309/325 of query aligns to 1923:2220/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
34% identity, 92% coverage: 10:309/325 of query aligns to 1:308/312 of 6ys6B
6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
34% identity, 92% coverage: 10:309/325 of query aligns to 1:308/312 of 6ypoA
- active site: R109 (= R114), H137 (= H142), Q140 (= Q145), T231 (≠ L229), P271 (= P270), G297 (= G298)
- binding uridine-5'-monophosphate: R58 (= R64), T59 (= T65), R109 (= R114), H137 (= H142), R170 (= R176), T171 (≠ V177), R232 (= R230), H270 (= H269), P271 (= P270), L272 (≠ G271)
6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate (see paper)
34% identity, 92% coverage: 10:309/325 of query aligns to 13:320/324 of 6yvbC
- active site: R121 (= R114), H149 (= H142), Q152 (= Q145), T243 (≠ L229), P283 (= P270), G309 (= G298)
- binding phosphoric acid mono(formamide)ester: S68 (= S62), T69 (= T63), R70 (= R64), T71 (= T65), R121 (= R114), H149 (= H142), Q152 (= Q145), P283 (= P270)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
33% identity, 91% coverage: 12:306/325 of query aligns to 2:296/304 of 4eknB
P49077 Aspartate carbamoyltransferase, chloroplastic; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 91% coverage: 13:309/325 of query aligns to 86:386/390 of P49077
- R136 (= R64) binding
- T137 (= T65) binding
- R187 (= R114) binding
- H215 (= H142) binding
- R248 (= R176) binding
- R310 (= R230) binding
Q09794 Multifunctional protein ura1; 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 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 91% coverage: 12:306/325 of query aligns to 1937:2233/2244 of Q09794
Sites not aligning to the query:
- 1119 modified: Phosphoserine
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
Query Sequence
>8500677 FitnessBrowser__Miya:8500677
MQHAQRPTWPHKDLLDVTQLTRAELFHLLDTAAQFHDINRRPVKKVPTLKGKSVVLFFAE
PSTRTKTSFDVAGKRLSADTFSLAKSGSSLSKGESLKDTALTLQAMTPDIIVIRHSSSGA
AQFLAERLDCSVVNAGDGWHAHPTQALLDCYSLRQVWGDTFEGRTLLILGDIAHSRVARS
NVHLLSSLGVKVRLCAPRTLLPAGVHNWPVTIFNRLDDAVQGVDAVMCLRLQLERQQAGL
LPDLREYAQRFCLSPRHLTMAAPSARVLHPGPMNRGLEISSVLADAPESLILDQVAAGVA
TRMAILFLLATRTGIEQTADNGGRA
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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