ID   PYRI_SACS2              Reviewed;         159 AA.
AC   Q9UX07;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Aspartate carbamoyltransferase regulatory chain;
GN   Name=pyrI; OrderedLocusNames=SSO0613;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=10701121; DOI=10.1139/g99-108;
RA   Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA   Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA   Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA   Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA   Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT   "Gene content and organization of a 281-kbp contig from the genome of the
RT   extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL   Genome 43:116-136(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- FUNCTION: Involved in allosteric regulation of aspartate
CC       carbamoyltransferase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Contains catalytic and regulatory chains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PyrI family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK40924.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAB57687.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y18930; CAB57687.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE006641; AAK40924.1; ALT_INIT; Genomic_DNA.
DR   PIR; E90208; E90208.
DR   RefSeq; WP_009991142.1; NC_002754.1.
DR   AlphaFoldDB; Q9UX07; -.
DR   SMR; Q9UX07; -.
DR   STRING; 273057.SSO0613; -.
DR   EnsemblBacteria; AAK40924; AAK40924; SSO0613.
DR   GeneID; 44129615; -.
DR   KEGG; sso:SSO0613; -.
DR   PATRIC; fig|273057.12.peg.621; -.
DR   eggNOG; arCOG04229; Archaea.
DR   HOGENOM; CLU_128576_0_0_2; -.
DR   InParanoid; Q9UX07; -.
DR   OMA; CPNRNCI; -.
DR   PhylomeDB; Q9UX07; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0009347; C:aspartate carbamoyltransferase complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; 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; 3.30.70.140; -; 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   PANTHER; PTHR35805; PTHR35805; 1.
DR   Pfam; PF01948; PyrI; 1.
DR   Pfam; PF02748; PyrI_C; 1.
DR   SUPFAM; SSF54893; SSF54893; 1.
DR   SUPFAM; SSF57825; SSF57825; 1.
DR   TIGRFAMs; TIGR00240; ATCase_reg; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Pyrimidine biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..159
FT                   /note="Aspartate carbamoyltransferase regulatory chain"
FT                   /id="PRO_0000142343"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   159 AA;  17982 MW;  CE20EDD33442EDC3 CRC64;
     MISSSKRDEL IVSKIRNGTV IDHIPAGRAL AVLRILGIRG SEGYRVALVM NVESKKIGRK
     DIVKIEDRVI DEKEASLITL IAPSATINII RDYVVTEKRH LEVPKQIRGL IKCPNPQCIT
     NNDVEAESRF ITISIKPLKL KCKYCEMYIT EDDVIRQIL