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Deoxycytidylate deaminase (EC 3.5.4.12) (dCMP deaminase)

 DCTD_RAT                Reviewed;         178 AA.
Q5M9G0;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 1.
22-NOV-2017, entry version 96.
RecName: Full=Deoxycytidylate deaminase;
EC=3.5.4.12;
AltName: Full=dCMP deaminase;
Name=Dctd;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Supplies the nucleotide substrate for thymidylate
synthetase. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: dCMP + H(2)O = dUMP + NH(3).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Allosteric enzyme whose activity is greatly
influenced by the end products of its metabolic pathway, dCTP and
dTTP. {ECO:0000250}.
-!- SUBUNIT: Homohexamer. {ECO:0000250}.
-!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
family. {ECO:0000305}.
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EMBL; BC087138; AAH87138.1; -; mRNA.
RefSeq; NP_001013904.2; NM_001013882.2.
RefSeq; NP_001154984.1; NM_001161512.1.
UniGene; Rn.105816; -.
ProteinModelPortal; Q5M9G0; -.
SMR; Q5M9G0; -.
STRING; 10116.ENSRNOP00000017670; -.
PaxDb; Q5M9G0; -.
GeneID; 290741; -.
KEGG; rno:290741; -.
CTD; 1635; -.
RGD; 1359671; Dctd.
eggNOG; KOG3127; Eukaryota.
eggNOG; COG2131; LUCA.
HOGENOM; HOG000015715; -.
HOVERGEN; HBG025823; -.
InParanoid; Q5M9G0; -.
KO; K01493; -.
PhylomeDB; Q5M9G0; -.
TreeFam; TF105971; -.
PRO; PR:Q5M9G0; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0004132; F:dCMP deaminase activity; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006231; P:dTMP biosynthetic process; IBA:GO_Central.
GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
CDD; cd01286; deoxycytidylate_deaminase; 1.
InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
InterPro; IPR002125; CMP_dCMP_dom.
InterPro; IPR016193; Cytidine_deaminase-like.
InterPro; IPR016473; dCMP_deaminase.
InterPro; IPR015517; dCMP_deaminase-rel.
InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
PANTHER; PTHR11086; PTHR11086; 1.
Pfam; PF00383; dCMP_cyt_deam_1; 1.
PIRSF; PIRSF006019; dCMP_deaminase; 1.
SUPFAM; SSF53927; SSF53927; 1.
PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
2: Evidence at transcript level;
Allosteric enzyme; Complete proteome; Hydrolase; Metal-binding;
Nucleotide biosynthesis; Phosphoprotein; Reference proteome; Zinc.
CHAIN 1 178 Deoxycytidylate deaminase.
/FTId=PRO_0000171694.
DOMAIN 14 145 CMP/dCMP-type deaminase.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
ACT_SITE 86 86 Proton donor. {ECO:0000250}.
METAL 84 84 Zinc; catalytic. {ECO:0000250}.
METAL 110 110 Zinc; catalytic. {ECO:0000250}.
METAL 113 113 Zinc; catalytic. {ECO:0000250}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000250|UniProtKB:P32321}.
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


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