ID   A0A2V3JMC2_9EURY        Unreviewed;       158 AA.
AC   A0A2V3JMC2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000256|ARBA:ARBA00021764, ECO:0000256|HAMAP-Rule:MF_00002};
GN   Name=pyrI {ECO:0000256|HAMAP-Rule:MF_00002};
GN   ORFNames=C4B59_06710 {ECO:0000313|EMBL:PXF61028.1};
OS   ANME-2 cluster archaeon.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinales incertae sedis; ANME-2 cluster.
OX   NCBI_TaxID=2056317 {ECO:0000313|EMBL:PXF61028.1, ECO:0000313|Proteomes:UP000248329};
RN   [1] {ECO:0000313|EMBL:PXF61028.1, ECO:0000313|Proteomes:UP000248329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E20ANME2 {ECO:0000313|EMBL:PXF61028.1};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in allosteric regulation of aspartate
CC       carbamoyltransferase. {ECO:0000256|ARBA:ARBA00002565,
CC       ECO:0000256|HAMAP-Rule:MF_00002}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00002};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00002};
CC   -!- SUBUNIT: Contains catalytic and regulatory chains. {ECO:0000256|HAMAP-
CC       Rule:MF_00002}.
CC   -!- SIMILARITY: Belongs to the PyrI family. {ECO:0000256|ARBA:ARBA00010498,
CC       ECO:0000256|HAMAP-Rule:MF_00002}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PXF61028.1}.
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DR   EMBL; PQXF01000009; PXF61028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V3JMC2; -.
DR   Proteomes; UP000248329; Unassembled WGS sequence.
DR   GO; GO:0009347; C:aspartate carbamoyltransferase complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.30.20; Aspartate carbamoyltransferase regulatory subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.140; Aspartate carbamoyltransferase regulatory subunit, N-terminal domain; 1.
DR   HAMAP; MF_00002; Asp_carb_tr_reg; 1.
DR   InterPro; IPR020545; Asp_carbamoyltransf_reg_N.
DR   InterPro; IPR002801; Asp_carbamoylTrfase_reg.
DR   InterPro; IPR020542; Asp_carbamoyltrfase_reg_C.
DR   InterPro; IPR036792; Asp_carbatrfase_reg_C_sf.
DR   InterPro; IPR036793; Asp_carbatrfase_reg_N_sf.
DR   NCBIfam; TIGR00240; ATCase_reg; 1.
DR   PANTHER; PTHR35805; ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN; 1.
DR   PANTHER; PTHR35805:SF1; ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN; 1.
DR   Pfam; PF01948; PyrI; 1.
DR   Pfam; PF02748; PyrI_C; 1.
DR   SUPFAM; SSF57825; Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain; 1.
DR   SUPFAM; SSF54893; Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00002};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_00002}; Reference proteome {ECO:0000313|Proteomes:UP000248329};
KW   Transferase {ECO:0000313|EMBL:PXF61028.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00002}.
FT   DOMAIN          13..101
FT                   /note="Aspartate carbamoyltransferase regulatory subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01948"
FT   DOMAIN          106..151
FT                   /note="Aspartate carbamoyltransferase regulatory subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02748"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00002"
SQ   SEQUENCE   158 AA;  17748 MW;  EC09C86E4D6CABBA CRC64;
     MKPKPGEPGD RELRVKRITN GTVIDHITAG QALNVLRILG ITDRPEEVVS VVMNVSDRKK
     DIVKIEGREL KPEEVDKIAL ISPDATINII RDYEVVEKHE VILPSQIEGV VRCINQNCIT
     NTDEPVKPRF VICRGERVEL HCVYCGSVIA DRIADFLI
//