ID   DCTD_CAEEL              Reviewed;         197 AA.
AC   P30648;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Probable deoxycytidylate deaminase;
DE            EC=3.5.4.12;
DE   AltName: Full=dCMP deaminase;
GN   ORFNames=ZK643.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=1538779; DOI=10.1038/356037a0;
RA   Sulston J., Du Z., Thomas K., Wilson R., Hillier L., Staden R.,
RA   Halloran N., Green P., Thierry-Mieg J., Qiu L., Dear S., Coulson A.,
RA   Craxton M., Durbin R., Berks M., Metzstein M., Hawkins T., Ainscough R.,
RA   Waterston R.;
RT   "The C. elegans genome sequencing project: a beginning.";
RL   Nature 356:37-41(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Supplies the nucleotide substrate for thymidylate synthetase.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCMP + H(+) + H2O = dUMP + NH4(+); Xref=Rhea:RHEA:22924,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57566, ChEBI:CHEBI:246422; EC=3.5.4.12;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; Z11126; CAA77473.1; -; Genomic_DNA.
DR   PIR; S23240; S23240.
DR   RefSeq; NP_498980.1; NM_066579.4.
DR   AlphaFoldDB; P30648; -.
DR   SMR; P30648; -.
DR   STRING; 6239.ZK643.2.1; -.
DR   ChEMBL; CHEMBL2448; -.
DR   EPD; P30648; -.
DR   PaxDb; 6239-ZK643-2; -.
DR   EnsemblMetazoa; ZK643.2.1; ZK643.2.1; WBGene00014034.
DR   GeneID; 191373; -.
DR   KEGG; cel:CELE_ZK643.2; -.
DR   UCSC; ZK643.2; c. elegans.
DR   AGR; WB:WBGene00014034; -.
DR   WormBase; ZK643.2; CE00441; WBGene00014034; -.
DR   eggNOG; KOG3127; Eukaryota.
DR   GeneTree; ENSGT00940000153676; -.
DR   HOGENOM; CLU_047993_1_1_1; -.
DR   InParanoid; P30648; -.
DR   OMA; CEIWVTH; -.
DR   OrthoDB; 5389250at2759; -.
DR   PhylomeDB; P30648; -.
DR   Reactome; R-CEL-499943; Interconversion of nucleotide di- and triphosphates.
DR   PRO; PR:P30648; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00014034; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004132; F:dCMP deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01286; deoxycytidylate_deaminase; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR015517; dCMP_deaminase-rel.
DR   InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
DR   PANTHER; PTHR11086:SF18; CYTIDINE AND DCMP DEAMINASE DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR11086; DEOXYCYTIDYLATE DEAMINASE-RELATED; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Nucleotide biosynthesis; Reference proteome;
KW   Zinc.
FT   CHAIN           1..197
FT                   /note="Probable deoxycytidylate deaminase"
FT                   /id="PRO_0000171695"
FT   DOMAIN          49..183
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        119
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   197 AA;  22528 MW;  33B6A723AD3F9FE7 CRC64;
     MVPPITSDEF CETSGCFGDS ANLHTTLERL KININSDAKK LVDTNGDLKK HQRFLRIAKV
     TSLRSKDPNT QVGCVIVDKD NCIVSVGYNG FPIGVDDDVF RWDKEDPEDN KHLYVVHAEM
     NAIINKRCTT LHDCTVYVTL FPCNKCAQML IQSRVKKVYF LENRDELAFR ASKKMLDHAR
     LPYEQIVMPQ EAYVIEL
//