Q91437 · PYR1_SQUAC
- ProteinMultifunctional protein CAD
- GeneCAD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2242 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Multifunctional protein that encodes the first 3 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5), aspartate transcarbamylase (ATCase; EC 2.1.3.2) and dihydroorotase (DHOase; EC 3.5.2.3). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate. In the last step, DHOase catalyzes the cyclization of carbamoyl aspartate to dihydroorotate.
Miscellaneous
GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).
Catalytic activity
- 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H+ + L-glutamate + phosphate
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 4 Mg2+ or Mn2+ ions per subunit.
Note: Binds 3 Zn2+ ions per subunit (for dihydroorotase activity).
Activity regulation
Allosterically regulated and controlled by phosphorylation. 5-phosphoribose 1-diphosphate is an activator while UMP is an inhibitor of the CPSase reaction.
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 44 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 222 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 224 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 252 | Nucleophile; for GATase activity | ||||
Sequence: C | ||||||
Binding site | 253 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 256 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 294 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 296 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 297 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Active site | 336 | For GATase activity | ||||
Sequence: H | ||||||
Active site | 338 | For GATase activity | ||||
Sequence: E | ||||||
Binding site | 518 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 558 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 564 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 565 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 595 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 602 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 628 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 629 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 630 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 671 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 671 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 671 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 685 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 685 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 685 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 685 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 685 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 687 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 687 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1093 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1132 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 1134 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 1139 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1164 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 1165 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 1166 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1167 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 1207 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 1207 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 1207 | Mn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 1219 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1219 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1219 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1219 | Mn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1219 | Mn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1221 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1221 | Mn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1478 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1478 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1480 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1482 | (S)-dihydroorotate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1512 | (S)-dihydroorotate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1563 | Zn2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 1563 | Zn2+ 3 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 1597 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1620 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1621 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1644 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1668 | (S)-dihydroorotate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 1693 | For DHOase activity | ||||
Sequence: D | ||||||
Binding site | 1693 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1697 | (S)-dihydroorotate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1709 | (S)-dihydroorotate (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Binding site | 1992 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1993 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 2020 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2041 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 2069 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 2072 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 2102 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 2163 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 2202 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 2203 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: P |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | amino acid binding | |
Molecular Function | aspartate carbamoyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | carbamoyl-phosphate synthase (ammonia) activity | |
Molecular Function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity | |
Molecular Function | dihydroorotase activity | |
Molecular Function | glutaminase activity | |
Molecular Function | zinc ion binding | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | citrulline biosynthetic process | |
Biological Process | glutamine metabolic process | |
Biological Process | UTP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional protein CAD
- Alternative names
Including 5 domains:
- Recommended nameGlutamine-dependent carbamoyl-phosphate synthase
- EC number
- Recommended nameGlutamine amidotransferase
- EC number
- Short namesGATase; GLNase
- Recommended nameAmmonium-dependent carbamoyl phosphate synthase
- EC number
- Short namesCPS; CPSase
- Recommended nameAspartate carbamoyltransferase
- EC number
- Recommended nameDihydroorotase
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Chondrichthyes > Elasmobranchii > Squalomorphii > Squaliformes > Squalidae > Squalus
Accessions
- Primary accessionQ91437
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000199508 | 1-2242 | Multifunctional protein CAD | |||
Sequence: MATLFLDDGSSFKGRLFGASSTVSGEVVFQTGMVGYPEALTDPSYLSQILVLTYPLIGNYGIPKDEEDEHGLSKWFESAKIHAAALVIGENSQNPSHWSSVRSLDQRLKEHGIPALEGIDTRSLTKKIREKGTLLGKLVIDGTDENSLPYDDPNKRHLVKEVSIKEPKVYHPSGNVKIMAVDCGMKYNQIRSLCKRGAAVTVVPWDYLFDSNEFDGLFISNGPGDPEYCQQTINNVKKAISEEKPKPLFGICLGHQILSLAIGAKTYKMKYGNRGHNQPCIHEGTQRCFYTSQNHGFAVEPCSLPRDWSVLFTNANDQSNEGIIHNSKPLFSVQFHPEHKAGPTDLVDLFDIFLECARDVKLGVNLDKTVKGRVISHYSFKNGTENSKTPPGRIQPHKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENVQSVLINPNIATVQTSKGLADKVYFLPITPEYVTQVIMNERPDGILLTFGGQTALNCGVELQKRGVLEKYHVRVLGTPVSSIEMTEDRKIFVEKMAEINEYVVPSEAAFTLEQAQGAAERLGYPVLVRAAFALGGLGSGFAQNKEELVTLVTQAFAHTSQILVDKSLKGWKEIEYEVVRDAYDNCITVCNMENVDPLGIHTGESIVVAPSQTLNDKEYNLLRTTAIKVIRHLGVVGECNIQYALSPESEQYFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPVLRNSVTNSTTANYEPSLDYCVVKVPRWDLSKFLRLSTKIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENCVGFDHTLKPASDEELETPTDKRIFVLAAALRAGYEIDRLYELTKIDKWFLHKMKNIVEYSLKLSELYMKDEVPRHDLLKVKRLGFSDKQIAMAIQSTELAVRRLRQEWKILPVVKQIDTVAAEWPAQTNYLYLTYNGEGHDLDFTKPHVMVIGSGVYRIGSSVEFDWCAVRCIQQLRKMGYKTRMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGIILSMGGQLPNNIAMDLHRQQCRILGTSPESIDTAENRFKFSRMLDTIGISQPRWKELSDTESSKQFCTKVGYPCLIRPSYVLSGVAMNVAYSDNDLEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVACDGVVIAVAISEHVENAGVHSGDATLVTPPQDLNQKTTERIKAIVHAIGQELQATGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDMIALATKVIMGEEVEPVGLMTGTGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKNILLSIGSYKNKSELLSTVQSLEQLGYNLYASLGTADFYTEHGVKIKAVDWPFEDTDNGCPLKERHRNIMDYLEENHFDLVINLSMRNSGGRRLSSFVTKGYRTRRLAVDYSVPLIIDIKCTKLFVEALRLVGDTPPVKTHIDSMSSHKLIRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTNPAITDQTSFALVQKLATAGARCDFALFLGASSDNADVLPLISNSAAGLKMYLNDTFSTLKMDNVSLWMEHFEKWPKHLPIVVHAERQTVAAILMVAQLYQRPVHICHVARKEEIQIIRAAKQKGVQVTCEVAPHHLFLNEEDLESIGHGKGQVRPMLSTKEDVNALWENLDVIDCFATDHAPHSVEEKNSDSPPPGYPGLETMLPLLLTAVSEGRLTIDDLVKRLYENPRKIFSLPVQENTYVEVDLEQEWIIPSYMQFTKSKWTPFEGKKVKGRVRRVVLRGEVAYIDGQVLVPPGYGQDVRAWPLGVPLPPPPTTVKTPEHSKPTQTETVRTRTASPRRLASSGPAVDARFHLPPRIHRCSDPGLPNAEGEYKEKPVKKFIEQDTVSQDGYIYPPPVSRLLSPQNLAAQAVPHPYSLLLHPFVGQHILSVKRFTKDQLSHLFNVAHNLRLTVQKDRSLDILKGKVMASMFYEVSTRTSSSFRAAMHRLGGSVIHFSEATSSVQKGESLLDSVQTMSCYVDVVVLRHPEPGAVELAAKHSRKPIINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLAYLLTLYRVNLRYVTPRNLRMPPNIIRFLASRGIKQEEFDSLEEALPDTDVLYMTRIQKERFASEEEYEACFGQFILTPHIMTKGKKKMVVMHPLPRVNEVSVEVDSDPRAAYFRQAENGMYVRMALLATVLGKF | ||||||
Modified residue | 1563 | N6-carboxylysine | ||||
Sequence: K |
Keywords
- PTM
Expression
Tissue specificity
Present in the testis but not in the liver.
Interaction
Subunit
Homohexamer.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-365 | GATase (Glutamine amidotransferase) | ||||
Sequence: MATLFLDDGSSFKGRLFGASSTVSGEVVFQTGMVGYPEALTDPSYLSQILVLTYPLIGNYGIPKDEEDEHGLSKWFESAKIHAAALVIGENSQNPSHWSSVRSLDQRLKEHGIPALEGIDTRSLTKKIREKGTLLGKLVIDGTDENSLPYDDPNKRHLVKEVSIKEPKVYHPSGNVKIMAVDCGMKYNQIRSLCKRGAAVTVVPWDYLFDSNEFDGLFISNGPGDPEYCQQTINNVKKAISEEKPKPLFGICLGHQILSLAIGAKTYKMKYGNRGHNQPCIHEGTQRCFYTSQNHGFAVEPCSLPRDWSVLFTNANDQSNEGIIHNSKPLFSVQFHPEHKAGPTDLVDLFDIFLECARDVKLGVN | ||||||
Domain | 177-363 | Glutamine amidotransferase type-1 | ||||
Sequence: KIMAVDCGMKYNQIRSLCKRGAAVTVVPWDYLFDSNEFDGLFISNGPGDPEYCQQTINNVKKAISEEKPKPLFGICLGHQILSLAIGAKTYKMKYGNRGHNQPCIHEGTQRCFYTSQNHGFAVEPCSLPRDWSVLFTNANDQSNEGIIHNSKPLFSVQFHPEHKAGPTDLVDLFDIFLECARDVKLG | ||||||
Region | 366-397 | Linker | ||||
Sequence: LDKTVKGRVISHYSFKNGTENSKTPPGRIQPH | ||||||
Region | 398-937 | CPSase A | ||||
Sequence: KVLILGSGGLSIGQAGEFDYSGSQAIKALKEENVQSVLINPNIATVQTSKGLADKVYFLPITPEYVTQVIMNERPDGILLTFGGQTALNCGVELQKRGVLEKYHVRVLGTPVSSIEMTEDRKIFVEKMAEINEYVVPSEAAFTLEQAQGAAERLGYPVLVRAAFALGGLGSGFAQNKEELVTLVTQAFAHTSQILVDKSLKGWKEIEYEVVRDAYDNCITVCNMENVDPLGIHTGESIVVAPSQTLNDKEYNLLRTTAIKVIRHLGVVGECNIQYALSPESEQYFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPVLRNSVTNSTTANYEPSLDYCVVKVPRWDLSKFLRLSTKIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENCVGFDHTLKPASDEELETPTDKRIFVLAAALRAGYEIDRLYELTKIDKWFLHKMKNIVEYSLKLSELYMKDEVPRHDLLKVKRLGFSDKQIAMAIQSTELAVRRLRQEWKILPVVKQIDTVAAEWPAQTNYLYLTYNGEGHDLDFTK | ||||||
Region | 398-1462 | CPSase (Carbamoyl-phosphate synthase) | ||||
Sequence: KVLILGSGGLSIGQAGEFDYSGSQAIKALKEENVQSVLINPNIATVQTSKGLADKVYFLPITPEYVTQVIMNERPDGILLTFGGQTALNCGVELQKRGVLEKYHVRVLGTPVSSIEMTEDRKIFVEKMAEINEYVVPSEAAFTLEQAQGAAERLGYPVLVRAAFALGGLGSGFAQNKEELVTLVTQAFAHTSQILVDKSLKGWKEIEYEVVRDAYDNCITVCNMENVDPLGIHTGESIVVAPSQTLNDKEYNLLRTTAIKVIRHLGVVGECNIQYALSPESEQYFIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPVLRNSVTNSTTANYEPSLDYCVVKVPRWDLSKFLRLSTKIGSSMKSVGEVMAIGRNFEEAFQKALRMVDENCVGFDHTLKPASDEELETPTDKRIFVLAAALRAGYEIDRLYELTKIDKWFLHKMKNIVEYSLKLSELYMKDEVPRHDLLKVKRLGFSDKQIAMAIQSTELAVRRLRQEWKILPVVKQIDTVAAEWPAQTNYLYLTYNGEGHDLDFTKPHVMVIGSGVYRIGSSVEFDWCAVRCIQQLRKMGYKTRMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGIILSMGGQLPNNIAMDLHRQQCRILGTSPESIDTAENRFKFSRMLDTIGISQPRWKELSDTESSKQFCTKVGYPCLIRPSYVLSGVAMNVAYSDNDLEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVACDGVVIAVAISEHVENAGVHSGDATLVTPPQDLNQKTTERIKAIVHAIGQELQATGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDMIALATKVIMGEEVEPVGLMTGTGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKNILLSIGSYKNKSELLSTVQSLEQLGYNLYASLGTADFYTEHGVKIKAVDWPFEDTDNGCPLKERHRNIMDYLEENHFDLVINLSMRNSGGRRLSSFVTKGYRTRRLAVDYSVPLIIDIKCTKLFVEALRLVGDTPPVKTHIDS | ||||||
Domain | 522-714 | ATP-grasp 1 | ||||
Sequence: VEKMAEINEYVVPSEAAFTLEQAQGAAERLGYPVLVRAAFALGGLGSGFAQNKEELVTLVTQAFAHTSQILVDKSLKGWKEIEYEVVRDAYDNCITVCNMENVDPLGIHTGESIVVAPSQTLNDKEYNLLRTTAIKVIRHLGVVGECNIQYALSPESEQYFIIEVNARLSRSSALASKATGYPLAYVAAKLAL | ||||||
Region | 938-1462 | CPSase B | ||||
Sequence: PHVMVIGSGVYRIGSSVEFDWCAVRCIQQLRKMGYKTRMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGIILSMGGQLPNNIAMDLHRQQCRILGTSPESIDTAENRFKFSRMLDTIGISQPRWKELSDTESSKQFCTKVGYPCLIRPSYVLSGVAMNVAYSDNDLEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVACDGVVIAVAISEHVENAGVHSGDATLVTPPQDLNQKTTERIKAIVHAIGQELQATGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDMIALATKVIMGEEVEPVGLMTGTGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKNILLSIGSYKNKSELLSTVQSLEQLGYNLYASLGTADFYTEHGVKIKAVDWPFEDTDNGCPLKERHRNIMDYLEENHFDLVINLSMRNSGGRRLSSFVTKGYRTRRLAVDYSVPLIIDIKCTKLFVEALRLVGDTPPVKTHIDS | ||||||
Domain | 1057-1248 | ATP-grasp 2 | ||||
Sequence: SRMLDTIGISQPRWKELSDTESSKQFCTKVGYPCLIRPSYVLSGVAMNVAYSDNDLEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVACDGVVIAVAISEHVENAGVHSGDATLVTPPQDLNQKTTERIKAIVHAIGQELQATGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDMIALATKVIM | ||||||
Domain | 1313-1469 | MGS-like | ||||
Sequence: FKIPKKNILLSIGSYKNKSELLSTVQSLEQLGYNLYASLGTADFYTEHGVKIKAVDWPFEDTDNGCPLKERHRNIMDYLEENHFDLVINLSMRNSGGRRLSSFVTKGYRTRRLAVDYSVPLIIDIKCTKLFVEALRLVGDTPPVKTHIDSMSSHKLI | ||||||
Region | 1463-1796 | DHOase (dihydroorotase) | ||||
Sequence: MSSHKLIRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTNPAITDQTSFALVQKLATAGARCDFALFLGASSDNADVLPLISNSAAGLKMYLNDTFSTLKMDNVSLWMEHFEKWPKHLPIVVHAERQTVAAILMVAQLYQRPVHICHVARKEEIQIIRAAKQKGVQVTCEVAPHHLFLNEEDLESIGHGKGQVRPMLSTKEDVNALWENLDVIDCFATDHAPHSVEEKNSDSPPPGYPGLETMLPLLLTAVSEGRLTIDDLVKRLYENPRKIFSLPVQENTYVEVDLEQEWIIPSYMQFTKSKWTPFEGKKVKGRVRRVVLR | ||||||
Region | 1797-1934 | Linker | ||||
Sequence: GEVAYIDGQVLVPPGYGQDVRAWPLGVPLPPPPTTVKTPEHSKPTQTETVRTRTASPRRLASSGPAVDARFHLPPRIHRCSDPGLPNAEGEYKEKPVKKFIEQDTVSQDGYIYPPPVSRLLSPQNLAAQAVPHPYSLL | ||||||
Region | 1829-1862 | Disordered | ||||
Sequence: PTTVKTPEHSKPTQTETVRTRTASPRRLASSGPA | ||||||
Compositional bias | 1835-1855 | Polar residues | ||||
Sequence: PEHSKPTQTETVRTRTASPRR | ||||||
Region | 1935-2242 | ATCase (Aspartate transcarbamylase) | ||||
Sequence: LHPFVGQHILSVKRFTKDQLSHLFNVAHNLRLTVQKDRSLDILKGKVMASMFYEVSTRTSSSFRAAMHRLGGSVIHFSEATSSVQKGESLLDSVQTMSCYVDVVVLRHPEPGAVELAAKHSRKPIINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLAYLLTLYRVNLRYVTPRNLRMPPNIIRFLASRGIKQEEFDSLEEALPDTDVLYMTRIQKERFASEEEYEACFGQFILTPHIMTKGKKKMVVMHPLPRVNEVSVEVDSDPRAAYFRQAENGMYVRMALLATVLGKF |
Sequence similarities
In the N-terminal section; belongs to the CarA family.
In the 2nd section; belongs to the CarB family.
In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,242
- Mass (Da)249,393
- Last updated1996-11-01 v1
- Checksum99F1986BA41244EA
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1835-1855 | Polar residues | ||||
Sequence: PEHSKPTQTETVRTRTASPRR |