SitesBLAST
Comparing Echvi_4661 FitnessBrowser__Cola:Echvi_4661 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)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 96% coverage: 7:300/307 of query aligns to 2:285/290 of 3r7lA
- active site: R49 (= R59), T50 (= T60), K77 (= K87), R99 (= R109), H127 (= H137), Q130 (= Q140), L210 (= L223), P249 (= P264), G277 (= G292)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S57), T48 (= T58), R49 (= R59), T50 (= T60), S74 (= S84), K77 (= K87), R99 (= R109), H127 (= H137), R160 (= R170), R211 (= R224), Q213 (= Q226), A250 (≠ G265)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
41% identity, 96% coverage: 7:300/307 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)
41% identity, 96% coverage: 7:300/307 of query aligns to 2:285/291 of 3r7fA
- active site: R49 (= R59), T50 (= T60), K77 (= K87), R99 (= R109), H127 (= H137), Q130 (= Q140), L210 (= L223), P249 (= P264), G277 (= G292)
- binding phosphoric acid mono(formamide)ester: S47 (= S57), T48 (= T58), R49 (= R59), T50 (= T60), R99 (= R109), H127 (= H137), Q130 (= Q140), P249 (= P264), A250 (≠ G265)
- binding phosphate ion: S11 (≠ N16), T12 (≠ E17), Q23 (≠ D28), K26 (= K31), E140 (= E150), R171 (≠ K181), K241 (≠ D256), H243 (≠ E258), K272 (≠ N287), K272 (≠ N287), K275 (≠ E290)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 96% coverage: 7:300/307 of query aligns to 2:285/291 of 3r7dA
- active site: R49 (= R59), T50 (= T60), K77 (= K87), R99 (= R109), H127 (= H137), Q130 (= Q140), L210 (= L223), P249 (= P264), G277 (= G292)
- binding phosphate ion: S11 (≠ N16), T12 (≠ E17), T73 (≠ S83), S74 (= S84), K77 (= K87), R171 (≠ K181)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
39% identity, 95% coverage: 8:300/307 of query aligns to 3:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S57), T49 (= T58), R50 (= R59), T51 (= T60), S75 (= S84), K78 (= K87), R100 (= R109), H127 (= H137), R160 (= R170), R210 (= R224), Q212 (= Q226), A253 (≠ G265)
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, 94% coverage: 15:303/307 of query aligns to 10:289/291 of 4bjhB
- active site: R47 (= R59), T48 (= T60), K75 (= K87), R97 (= R109), H126 (= H137), Q129 (= Q140)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S57), T46 (= T58), R47 (= R59), T48 (= T60), R97 (= R109), H126 (= H137), R159 (= R170), V160 (= V171), R213 (= R224), Q215 (= Q226), G251 (= G265)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
39% identity, 94% coverage: 15:303/307 of query aligns to 10:289/291 of 3d6nB
- active site: R47 (= R59), T48 (= T60), K75 (= K87), R97 (= R109), H126 (= H137), Q129 (= Q140)
- binding citrate anion: T48 (= T60), R97 (= R109), H126 (= H137), R159 (= R170), V160 (= V171), R213 (= R224), G251 (= G265)
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
34% identity, 97% coverage: 7:305/307 of query aligns to 6:305/307 of 5g1nE
- active site: R57 (= R59), T58 (= T60), K85 (= K87), R106 (= R109), H134 (= H137), Q137 (= Q140), T227 (≠ L223), P266 (= P264), G292 (= G292)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S57), T56 (= T58), R57 (= R59), T58 (= T60), S82 (= S84), K85 (= K87), R106 (= R109), H134 (= H137), R167 (= R170), R228 (= R224), Q230 (= Q226), M267 (≠ G265)
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, 99% coverage: 1:305/307 of query aligns to 1918:2223/2225 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.
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
36% identity, 98% coverage: 7:306/307 of query aligns to 5:306/307 of 1ml4A
- active site: R56 (= R59), T57 (= T60), K85 (= K87), R106 (= R109), H134 (= H137), Q137 (= Q140), T227 (≠ L223), P266 (= P264), G292 (= G292)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S57), T55 (= T58), R56 (= R59), T57 (= T60), R106 (= R109), H134 (= H137), R167 (= R170), T168 (≠ V171), R228 (= R224), L267 (≠ G265)
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, 99% coverage: 1:305/307 of query aligns to 1918:2223/2225 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
5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
33% identity, 97% coverage: 7:305/307 of query aligns to 3:290/292 of 5g1pA
- active site: R54 (= R59), T55 (= T60), K82 (= K87), R103 (= R109), H131 (= H137), Q134 (= Q140), T223 (≠ L223), P251 (= P264), G277 (= G292)
- binding phosphoric acid mono(formamide)ester: S52 (= S57), T53 (= T58), R54 (= R59), T55 (= T60), R103 (= R109), Q134 (= Q140), M252 (≠ G265)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
38% identity, 96% coverage: 7:300/307 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)
35% identity, 95% coverage: 13:303/307 of query aligns to 91:386/390 of P49077
- R136 (= R59) binding
- T137 (= T60) binding
- R187 (= R109) binding
- H215 (= H137) binding
- R248 (= R170) binding
- R310 (= R224) binding
6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
35% identity, 92% coverage: 23:303/307 of query aligns to 23:308/312 of 6ys6B
6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
35% identity, 92% coverage: 23:303/307 of query aligns to 23:308/312 of 6ypoA
- active site: R109 (= R109), H137 (= H137), Q140 (= Q140), T231 (≠ L223), P271 (= P264), G297 (= G292)
- binding uridine-5'-monophosphate: R58 (= R59), T59 (= T60), R109 (= R109), H137 (= H137), R170 (= R170), T171 (≠ V171), R232 (= R224), H270 (= H263), P271 (= P264), L272 (≠ G265)
6yvbC Arabidopsis aspartate transcarbamoylase complex with carbamoyl phosphate (see paper)
35% identity, 92% coverage: 23:303/307 of query aligns to 35:320/324 of 6yvbC
- active site: R121 (= R109), H149 (= H137), Q152 (= Q140), T243 (≠ L223), P283 (= P264), G309 (= G292)
- binding phosphoric acid mono(formamide)ester: S68 (= S57), T69 (= T58), R70 (= R59), T71 (= T60), R121 (= R109), H149 (= H137), Q152 (= Q140), P283 (= P264)
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)
33% identity, 99% coverage: 4:306/307 of query aligns to 1920:2223/2225 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)
34% identity, 98% coverage: 4:303/307 of query aligns to 5:304/311 of P0A786
- R55 (= R59) binding
- T56 (= T60) binding
- R106 (= R109) binding
- H135 (= H137) binding
- Q138 (= Q140) binding
- L268 (≠ G265) binding
- P269 (= P266) 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, 98% coverage: 4:303/307 of query aligns to 4:303/310 of 2ipoA
- active site: R54 (= R59), T55 (= T60), K84 (= K87), R105 (= R109), H134 (= H137), Q137 (= Q140), T228 (≠ L223), P266 (= P264), G292 (= G292)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S57), T53 (= T58), R54 (= R59), T55 (= T60), R105 (= R109), H134 (= H137), R167 (= R170), T168 (≠ V171), R229 (= R224), L267 (≠ G265)
Query Sequence
>Echvi_4661 FitnessBrowser__Cola:Echvi_4661
MQQLSTKHLLGIKGLNEADIQLIFETADNFKEVINRPIKKVPSLRDITIANVFFENSTRT
RLSFELAEKRLSADVINFSSSNSSVKKGETLVDTVNNILSMKVDMVVMRHSSPGAPHFLS
QNIDANIVNAGDGTHEHPTQALLDAFSIREKLGDVAGKKVAIIGDILHSRVALSNIFCLQ
KLGAEVMVCGPITLLPKYISSLGVKVELDVKKALEWCDVANVLRIQLERQQIKYFPSLRE
YSLYYGVDKKLLDQLDKEIVIMHPGPINRGVELNSDVADSEHSIILNQVENGVAVRMAVL
YLLAGVK
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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