ID   DCTD_YEAST              Reviewed;         312 AA.
AC   P06773; D3DL94;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Deoxycytidylate deaminase {ECO:0000305};
DE            EC=3.5.4.12 {ECO:0000305|PubMed:3023902};
DE   AltName: Full=dCMP deaminase {ECO:0000303|PubMed:3023902};
GN   Name=DCD1 {ECO:0000303|PubMed:3023902}; OrderedLocusNames=YHR144C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=3023902; DOI=10.1128/mcb.6.5.1711-1721.1986;
RA   McIntosh E.M., Haynes R.H.;
RT   "Sequence and expression of the dCMP deaminase gene (DCD1) of Saccharomyces
RT   cerevisiae.";
RL   Mol. Cell. Biol. 6:1711-1721(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of dCMP to yield dUMP,
CC       the nucleotide substrate for thymidylate synthetase.
CC       {ECO:0000305|PubMed:3023902}.
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         Evidence={ECO:0000305|PubMed:3023902};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22925;
CC         Evidence={ECO:0000305|PubMed:3023902};
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   -!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; M13010; AAA34561.1; -; Genomic_DNA.
DR   EMBL; U10397; AAB68985.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06838.1; -; Genomic_DNA.
DR   PIR; S46762; S46762.
DR   RefSeq; NP_012014.1; NM_001179275.1.
DR   AlphaFoldDB; P06773; -.
DR   SMR; P06773; -.
DR   BioGRID; 36578; 199.
DR   DIP; DIP-4028N; -.
DR   IntAct; P06773; 1.
DR   MINT; P06773; -.
DR   STRING; 4932.YHR144C; -.
DR   MaxQB; P06773; -.
DR   PaxDb; 4932-YHR144C; -.
DR   PeptideAtlas; P06773; -.
DR   EnsemblFungi; YHR144C_mRNA; YHR144C; YHR144C.
DR   GeneID; 856548; -.
DR   KEGG; sce:YHR144C; -.
DR   AGR; SGD:S000001187; -.
DR   SGD; S000001187; DCD1.
DR   VEuPathDB; FungiDB:YHR144C; -.
DR   eggNOG; KOG3127; Eukaryota.
DR   GeneTree; ENSGT00940000153676; -.
DR   HOGENOM; CLU_047993_0_0_1; -.
DR   InParanoid; P06773; -.
DR   OMA; PPLRPDW; -.
DR   OrthoDB; 178124at2759; -.
DR   BioCyc; MetaCyc:YHR144C-MONOMER; -.
DR   BioCyc; YEAST:YHR144C-MONOMER; -.
DR   BioGRID-ORCS; 856548; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P06773; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P06773; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0004132; F:dCMP deaminase activity; IMP:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IMP:SGD.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IMP:SGD.
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   1: Evidence at protein level;
KW   Allosteric enzyme; Hydrolase; Metal-binding; Nucleotide biosynthesis;
KW   Reference proteome; Zinc.
FT   CHAIN           1..312
FT                   /note="Deoxycytidylate deaminase"
FT                   /id="PRO_0000171697"
FT   DOMAIN          162..291
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        235
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        78
FT                   /note="V -> A (in Ref. 1; AAA34561)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   312 AA;  35646 MW;  780B47CDA561D24B CRC64;
     MLIGVSGTKF CGCEDVINML VDHFHFELLN HLDNPEEILD YATKNYTKNS VIFLEKLSLL
     EKLEKRPFFV HLSIDAPVTT RVALYRKTTQ AESLSLEQII QAIDQHDFQP EGIKLREKSH
     LRFKIVNEDR RGRRQSLINN ITTQLKILDD KEKQMAPLMR PSWDSYFMKL ATLAASRSNC
     MKRRVGCVIV RECRVIATGY NGTPRHLTNC FNGGCPRCND GDSRNLHTCL CLHAEENALL
     EAGRDRVGQN ATLYCDTCPC LTCSVKIVQT GISEVVYSQS YRMDEESFKV LKNAGITVRQ
     FSFTEEPRIV MI
//