ID   DCD_HALLT               Reviewed;         203 AA.
AC   B9LSY2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   02-SEP-2026, entry version 78.
DE   RecName: Full=dCTP deaminase {ECO:0000255|HAMAP-Rule:MF_00146};
DE            EC=3.5.4.13 {ECO:0000255|HAMAP-Rule:MF_00146};
DE   AltName: Full=Deoxycytidine triphosphate deaminase {ECO:0000255|HAMAP-Rule:MF_00146};
GN   Name=dcd {ECO:0000255|HAMAP-Rule:MF_00146};
GN   OrderedLocusNames=Hlac_0445;
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS   34).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Halobacteria; Halobacteriales; Haloferacaceae; Halorubrum.
OX   NCBI_TaxID=416348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX   PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA   Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA   Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA   Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA   Woese C.R., Kyrpides N.C.;
RT   "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT   strain ACAM 34.";
RL   Stand. Genomic Sci. 11:70-70(2016).
CC   -!- FUNCTION: Catalyzes the deamination of dCTP to dUTP.
CC       {ECO:0000255|HAMAP-Rule:MF_00146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCTP + H2O + H(+) = dUTP + NH4(+); Xref=Rhea:RHEA:22680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:61481, ChEBI:CHEBI:61555; EC=3.5.4.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00146};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 1/2. {ECO:0000255|HAMAP-Rule:MF_00146}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00146}.
CC   -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00146}.
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DR   EMBL; CP001365; ACM56047.1; -; Genomic_DNA.
DR   RefSeq; WP_012659682.1; NC_012029.1.
DR   AlphaFoldDB; B9LSY2; -.
DR   SMR; B9LSY2; -.
DR   GeneID; 7401063; -.
DR   KEGG; hla:Hlac_0445; -.
DR   eggNOG; arCOG04048; Archaea.
DR   HOGENOM; CLU_087476_2_1_2; -.
DR   UniPathway; UPA00610; UER00665.
DR   Proteomes; UP000000740; Chromosome 1.
DR   GO; GO:0008829; F:dCTP deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006229; P:dUTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IEA:TreeGrafter.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   FunFam; 2.70.40.10:FF:000005; dCTP deaminase, dUMP-forming; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   HAMAP; MF_00146; dCTP_deaminase; 1.
DR   InterPro; IPR011962; dCTP_deaminase.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   NCBIfam; TIGR02274; dCTP_deam; 1.
DR   PANTHER; PTHR42680; DCTP DEAMINASE; 1.
DR   PANTHER; PTHR42680:SF3; DCTP DEAMINASE; 1.
DR   Pfam; PF22769; DCD; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nucleotide metabolism; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..203
FT                   /note="dCTP deaminase"
FT                   /id="PRO_1000123148"
FT   REGION          164..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        133
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         105..110
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         123
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         131..133
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         152
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         166
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         173
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
FT   BINDING         177
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00146"
SQ   SEQUENCE   203 AA;  22142 MW;  08B3B9786BC5337C CRC64;
     MILSDADILD RLAEGDLVVE PLDDVDQQVQ PASVDLRLGE RFLEFQRTNI PCIHPTEADE
     VGDYVTETRV PEGEEFILHP GDFVLGTTTE RVEIPPDLLA TVQGRSSLGR LAIVIHATAG
     IVDPGYKGQI TLELSNLGTA PVALTPGMRV SQLIFTELKS PAKRPYGVER GSKYQDQDGP
     QASRIGSDPE FHSDENQAAE HES
//