SitesBLAST
Comparing CA265_RS14660 FitnessBrowser__Pedo557:CA265_RS14660 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)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
40% identity, 94% coverage: 12:304/311 of query aligns to 3:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S61), T49 (= T62), R50 (= R63), T51 (= T64), S75 (= S88), K78 (= K91), R100 (= R113), H127 (= H141), R160 (= R174), R210 (= R228), Q212 (= Q230), A253 (≠ G269)
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)
39% identity, 96% coverage: 11:309/311 of query aligns to 2:291/291 of 4bjhB
- active site: R47 (= R63), T48 (= T64), K75 (= K91), R97 (= R113), H126 (= H141), Q129 (= Q144)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S61), T46 (= T62), R47 (= R63), T48 (= T64), R97 (= R113), H126 (= H141), R159 (= R174), V160 (= V175), R213 (= R228), Q215 (= Q230), G251 (= G269)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
39% identity, 96% coverage: 11:309/311 of query aligns to 2:291/291 of 3d6nB
- active site: R47 (= R63), T48 (= T64), K75 (= K91), R97 (= R113), H126 (= H141), Q129 (= Q144)
- binding citrate anion: T48 (= T64), R97 (= R113), H126 (= H141), R159 (= R174), V160 (= V175), R213 (= R228), G251 (= G269)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
40% identity, 95% coverage: 11:304/311 of query aligns to 2:285/290 of 3r7lA
- active site: R49 (= R63), T50 (= T64), K77 (= K91), R99 (= R113), H127 (= H141), Q130 (= Q144), L210 (= L227), P249 (= P268), G277 (= G296)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S61), T48 (= T62), R49 (= R63), T50 (= T64), S74 (= S88), K77 (= K91), R99 (= R113), H127 (= H141), R160 (= R174), R211 (= R228), Q213 (= Q230), A250 (≠ G269)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
40% identity, 95% coverage: 11:304/311 of query aligns to 2:285/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
40% identity, 95% coverage: 11:304/311 of query aligns to 2:285/291 of 3r7fA
- active site: R49 (= R63), T50 (= T64), K77 (= K91), R99 (= R113), H127 (= H141), Q130 (= Q144), L210 (= L227), P249 (= P268), G277 (= G296)
- binding phosphoric acid mono(formamide)ester: S47 (= S61), T48 (= T62), R49 (= R63), T50 (= T64), R99 (= R113), H127 (= H141), Q130 (= Q144), P249 (= P268), A250 (≠ G269)
- binding phosphate ion: S11 (≠ N20), T12 (≠ R21), Q23 (≠ D32), K26 (= K35), E140 (≠ Q154), R171 (= R185), K241 (≠ D260), H243 (≠ E262), K272 (≠ E291), K272 (≠ E291), K275 (≠ E294)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
40% identity, 95% coverage: 11:304/311 of query aligns to 2:285/291 of 3r7dA
- active site: R49 (= R63), T50 (= T64), K77 (= K91), R99 (= R113), H127 (= H141), Q130 (= Q144), L210 (= L227), P249 (= P268), G277 (= G296)
- binding phosphate ion: S11 (≠ N20), T12 (≠ R21), T73 (≠ S87), S74 (= S88), K77 (= K91), R171 (= R185)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
36% identity, 95% coverage: 11:304/311 of query aligns to 6:300/307 of 5g1nE
- active site: R57 (= R63), T58 (= T64), K85 (= K91), R106 (= R113), H134 (= H141), Q137 (= Q144), T227 (≠ L227), P266 (= P268), G292 (= G296)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S61), T56 (= T62), R57 (= R63), T58 (= T64), S82 (= S88), K85 (= K91), R106 (= R113), H134 (= H141), R167 (= R174), R228 (= R228), Q230 (= Q230), M267 (≠ G269)
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)
36% identity, 95% coverage: 8:304/311 of query aligns to 1921:2218/2225 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)
37% identity, 95% coverage: 11:307/311 of query aligns to 5:303/307 of 1ml4A
- active site: R56 (= R63), T57 (= T64), K85 (= K91), R106 (= R113), H134 (= H141), Q137 (= Q144), T227 (≠ L227), P266 (= P268), G292 (= G296)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S61), T55 (= T62), R56 (= R63), T57 (= T64), R106 (= R113), H134 (= H141), R167 (= R174), T168 (≠ V175), R228 (= R228), L267 (≠ G269)
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)
36% identity, 95% coverage: 8:304/311 of query aligns to 1921:2218/2225 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
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
35% identity, 95% coverage: 11:304/311 of query aligns to 3:285/292 of 5g1pA
- active site: R54 (= R63), T55 (= T64), K82 (= K91), R103 (= R113), H131 (= H141), Q134 (= Q144), T223 (≠ L227), P251 (= P268), G277 (= G296)
- binding phosphoric acid mono(formamide)ester: S52 (= S61), T53 (= T62), R54 (= R63), T55 (= T64), R103 (= R113), Q134 (= Q144), M252 (≠ G269)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
37% identity, 95% coverage: 11:304/311 of query aligns to 2:296/304 of 4eknB
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, 98% coverage: 8:311/311 of query aligns to 1920:2224/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
32% identity, 99% coverage: 1:309/311 of query aligns to 6:316/316 of 8bplA
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
34% identity, 97% coverage: 5:307/311 of query aligns to 2:304/311 of P0A786
- R55 (= R63) binding
- T56 (= T64) binding
- R106 (= R113) binding
- H135 (= H141) binding
- Q138 (= Q144) binding
- L268 (≠ G269) binding
- P269 (= P270) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
34% identity, 97% coverage: 5:307/311 of query aligns to 1:303/310 of 2ipoA
- active site: R54 (= R63), T55 (= T64), K84 (= K91), R105 (= R113), H134 (= H141), Q137 (= Q144), T228 (≠ L227), P266 (= P268), G292 (= G296)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S61), T53 (= T62), R54 (= R63), T55 (= T64), R105 (= R113), H134 (= H141), R167 (= R174), T168 (≠ V175), R229 (= R228), L267 (≠ G269)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
34% identity, 97% coverage: 5:307/311 of query aligns to 1:303/310 of 2h3eA
- active site: R54 (= R63), T55 (= T64), K84 (= K91), R105 (= R113), H134 (= H141), Q137 (= Q144), T228 (≠ L227), P266 (= P268), G292 (= G296)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S61), T53 (= T62), R54 (= R63), T55 (= T64), R105 (= R113), H134 (= H141), R167 (= R174), R229 (= R228), L267 (≠ G269)
2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
34% identity, 97% coverage: 5:307/311 of query aligns to 1:303/310 of 2fzkA
- active site: R54 (= R63), T55 (= T64), K84 (= K91), R105 (= R113), H134 (= H141), Q137 (= Q144), T228 (≠ L227), P266 (= P268), G292 (= G296)
- binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T64), H134 (= H141), Q137 (= Q144), T168 (≠ V175), R229 (= R228), P266 (= P268), L267 (≠ G269), R296 (= R300)
2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
34% identity, 97% coverage: 5:307/311 of query aligns to 1:303/310 of 2fzgA
- active site: R54 (= R63), T55 (= T64), K84 (= K91), R105 (= R113), H134 (= H141), Q137 (= Q144), T228 (≠ L227), P266 (= P268), G292 (= G296)
- binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S61), R54 (= R63), T55 (= T64), R105 (= R113), H134 (= H141), R167 (= R174), T168 (≠ V175), R229 (= R228), P266 (= P268), L267 (≠ G269)
Query Sequence
>CA265_RS14660 FitnessBrowser__Pedo557:CA265_RS14660
MKMAAEKLSTRHLLGIKDINRNDIELIFETADNFKEVINRPIKKVPSLRDITIANIFFEN
STRTKLSFELAEKRLSADVVNFAASSSSVSKGETLIDTVNNILSMKVDMVVMRHPYAGAG
QFLSKHVKAQIVNAGDGAHEHPTQALLDAFSIRQKLGDVAGKKVVIVGDILHSRVAISNI
LCLQRLGAEVMVCGPTTLIPKHIHQLGVKVEHNLIKALNWCDVANMLRIQLERQDIKYFP
SLREYAMMYGLNKQILDNLDKEIIVMHPGPINRGVEITSDVADSKQSIILEQVENGVAVR
MAVLYLLASQG
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