ID   DCTD_RAT                Reviewed;         178 AA.
AC   Q5M9G0;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Deoxycytidylate deaminase;
DE            EC=3.5.4.12;
DE   AltName: Full=dCMP deaminase;
GN   Name=Dctd;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   -!- ACTIVITY REGULATION: Allosteric enzyme whose activity is greatly
CC       influenced by the end products of its metabolic pathway, dCTP and dTTP.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; BC087138; AAH87138.1; -; mRNA.
DR   RefSeq; NP_001013904.2; NM_001013882.2.
DR   RefSeq; NP_001154984.1; NM_001161512.1.
DR   AlphaFoldDB; Q5M9G0; -.
DR   SMR; Q5M9G0; -.
DR   STRING; 10116.ENSRNOP00000017670; -.
DR   PaxDb; Q5M9G0; -.
DR   GeneID; 290741; -.
DR   KEGG; rno:290741; -.
DR   CTD; 1635; -.
DR   RGD; 1359671; Dctd.
DR   eggNOG; KOG3127; Eukaryota.
DR   InParanoid; Q5M9G0; -.
DR   OrthoDB; 1569973at2759; -.
DR   PhylomeDB; Q5M9G0; -.
DR   TreeFam; TF105971; -.
DR   Reactome; R-RNO-499943; Interconversion of nucleotide di- and triphosphates.
DR   PRO; PR:Q5M9G0; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0004132; F:dCMP deaminase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
DR   CDD; cd01286; deoxycytidylate_deaminase; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR016473; dCMP_deaminase.
DR   InterPro; IPR015517; dCMP_deaminase-rel.
DR   InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
DR   PANTHER; PTHR11086; PTHR11086; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   PIRSF; PIRSF006019; dCMP_deaminase; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Hydrolase; Metal-binding; Nucleotide biosynthesis;
KW   Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..178
FT                   /note="Deoxycytidylate deaminase"
FT                   /id="PRO_0000171694"
FT   DOMAIN          14..145
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        86
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32321"
SQ   SEQUENCE   178 AA;  20059 MW;  A53ED5C676965029 CRC64;
     MSDISCKKRD DYLEWPEYFM AVAFLSAQRS KDPSSQVGAC IVNTENKIVG IGYNGMPNGC
     SDDLLPWRRT AENKLDTKYP YVCHAELNAI MNKNSADVKG CSMYVALFPC NECAKLIIQA
     GIKEVIFMSD KYHDSEETTA ARLLFKLAGV TFRKFTPKYS KIVIDFDSIN SRPSQKPQ