SitesBLAST
Comparing RR42_RS15860 FitnessBrowser__Cup4G11:RR42_RS15860 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)
42% identity, 93% coverage: 16:315/323 of query aligns to 1:285/291 of 3r7fA
- active site: R49 (= R71), T50 (= T72), K77 (= K99), R99 (= R121), H127 (= H151), Q130 (= Q154), L210 (= L238), P249 (= P279), G277 (= G307)
- binding phosphoric acid mono(formamide)ester: S47 (= S69), T48 (= T70), R49 (= R71), T50 (= T72), R99 (= R121), H127 (= H151), Q130 (= Q154), P249 (= P279), A250 (≠ G280)
- binding phosphate ion: S11 (= S26), T12 (≠ R27), Q23 (≠ S38), K26 (≠ V41), E140 (≠ H164), R171 (≠ T195), K241 (= K271), H243 (≠ D273), K272 (≠ N302), K272 (≠ N302), K275 (≠ T305)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
42% identity, 93% coverage: 16:315/323 of query aligns to 1:285/291 of 3r7dA
- active site: R49 (= R71), T50 (= T72), K77 (= K99), R99 (= R121), H127 (= H151), Q130 (= Q154), L210 (= L238), P249 (= P279), G277 (= G307)
- binding phosphate ion: S11 (= S26), T12 (≠ R27), T73 (≠ S95), S74 (= S96), K77 (= K99), R171 (≠ T195)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
42% identity, 93% coverage: 16:315/323 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)
42% identity, 93% coverage: 16:315/323 of query aligns to 1:285/290 of 3r7lA
- active site: R49 (= R71), T50 (= T72), K77 (= K99), R99 (= R121), H127 (= H151), Q130 (= Q154), L210 (= L238), P249 (= P279), G277 (= G307)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S69), T48 (= T70), R49 (= R71), T50 (= T72), S74 (= S96), K77 (= K99), R99 (= R121), H127 (= H151), R160 (= R184), R211 (= R239), Q213 (= Q241), A250 (≠ G280)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
39% identity, 93% coverage: 16:315/323 of query aligns to 1:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S69), T49 (= T70), R50 (= R71), T51 (= T72), S75 (= S96), K78 (= K99), R100 (= R121), H127 (= H151), R160 (= R184), R210 (= R239), Q212 (= Q241), A253 (≠ G280)
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)
40% identity, 93% coverage: 16:314/323 of query aligns to 1:285/291 of 4bjhB
- active site: R47 (= R71), T48 (= T72), K75 (= K99), R97 (= R121), H126 (= H151), Q129 (= Q154)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S69), T46 (= T70), R47 (= R71), T48 (= T72), R97 (= R121), H126 (= H151), R159 (= R184), V160 (= V185), R213 (= R239), Q215 (= Q241), G251 (= G280)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
40% identity, 93% coverage: 16:314/323 of query aligns to 1:285/291 of 3d6nB
- active site: R47 (= R71), T48 (= T72), K75 (= K99), R97 (= R121), H126 (= H151), Q129 (= Q154)
- binding citrate anion: T48 (= T72), R97 (= R121), H126 (= H151), R159 (= R184), V160 (= V185), R213 (= R239), G251 (= G280)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
38% identity, 93% coverage: 16:315/323 of query aligns to 1:296/304 of 4eknB
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)
35% identity, 94% coverage: 17:320/323 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.
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, 94% coverage: 17:320/323 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
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
35% identity, 94% coverage: 17:321/323 of query aligns to 6:306/307 of 5g1nE
- active site: R57 (= R71), T58 (= T72), K85 (= K99), R106 (= R121), H134 (= H151), Q137 (= Q154), T227 (≠ L238), P266 (= P279), G292 (= G307)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S69), T56 (= T70), R57 (= R71), T58 (= T72), S82 (= S96), K85 (= K99), R106 (= R121), H134 (= H151), R167 (= R184), R228 (= R239), Q230 (= Q241), M267 (≠ G280)
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
33% identity, 94% coverage: 17:321/323 of query aligns to 3:291/292 of 5g1pA
- active site: R54 (= R71), T55 (= T72), K82 (= K99), R103 (= R121), H131 (= H151), Q134 (= Q154), T223 (≠ L238), P251 (= P279), G277 (= G307)
- binding phosphoric acid mono(formamide)ester: S52 (= S69), T53 (= T70), R54 (= R71), T55 (= T72), R103 (= R121), Q134 (= Q154), M252 (≠ G280)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
36% identity, 94% coverage: 17:320/323 of query aligns to 5:305/307 of 1ml4A
- active site: R56 (= R71), T57 (= T72), K85 (= K99), R106 (= R121), H134 (= H151), Q137 (= Q154), T227 (≠ L238), P266 (= P279), G292 (= G307)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S69), T55 (= T70), R56 (= R71), T57 (= T72), R106 (= R121), H134 (= H151), R167 (= R184), T168 (≠ V185), R228 (= R239), L267 (≠ G280)
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)
33% identity, 95% coverage: 17:323/323 of query aligns to 1918:2221/2224 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
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
35% identity, 93% coverage: 17:318/323 of query aligns to 7:303/310 of 2hseA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding aspartic acid: R54 (= R71), T55 (= T72), S58 (≠ T75), R105 (= R121), H134 (= H151), Q137 (= Q154), R167 (= R184), R229 (= R239), Q231 (= Q241), L267 (≠ G280), P268 (= P281), A289 (≠ V304), R296 (= R311)
- binding phosphonoacetamide: S52 (= S69), T53 (= T70), R54 (= R71), T55 (= T72), R105 (= R121), L267 (≠ G280)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
35% identity, 93% coverage: 17:318/323 of query aligns to 7:303/310 of 2a0fA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding phosphonoacetamide: R54 (= R71), T55 (= T72), H134 (= H151), Q137 (= Q154), L267 (≠ G280)
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
35% identity, 93% coverage: 17:318/323 of query aligns to 7:303/310 of 2ipoA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S69), T53 (= T70), R54 (= R71), T55 (= T72), R105 (= R121), H134 (= H151), R167 (= R184), T168 (≠ V185), R229 (= R239), L267 (≠ G280)
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, 93% coverage: 17:318/323 of query aligns to 7:303/310 of 2h3eA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S69), T53 (= T70), R54 (= R71), T55 (= T72), R105 (= R121), H134 (= H151), R167 (= R184), R229 (= R239), L267 (≠ G280)
2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
35% identity, 93% coverage: 17:318/323 of query aligns to 7:303/310 of 2fzkA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T72), H134 (= H151), Q137 (= Q154), T168 (≠ V185), R229 (= R239), P266 (= P279), L267 (≠ G280), R296 (= R311)
2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
35% identity, 93% coverage: 17:318/323 of query aligns to 7:303/310 of 2fzgA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S69), R54 (= R71), T55 (= T72), R105 (= R121), H134 (= H151), R167 (= R184), T168 (≠ V185), R229 (= R239), P266 (= P279), L267 (≠ G280)
Query Sequence
>RR42_RS15860 FitnessBrowser__Cup4G11:RR42_RS15860
MIKTFRNPQLTKNGELKHLLSIEGLSREMVAHILDTASQFVSLSDSDREVKKVPLLRGKS
VFNLFFENSTRTRTTFEIAAKRLSADVLNLNINASSTSKGESLLDTINNLSAMSADMFVV
RHASSGAPYLIAEHVAPHVHVINAGDGRHAHPTQGLLDMYTIRHYKKDFTNLTVAIVGDI
LHSRVARSDIHALTTLGVPEVRAIGPRTLLPSGLEQMGVRVFHNMEEGMKGVDVVIMLRL
QNERMSGALLPSAQEYFKAYGLTPERLALAKPDAIVMHPGPMNRGVEIDSAVADGPQSVI
LNQVTFGIAVRMAVMGIVAGNHD
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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