ID   DCK1_FOWPN              Reviewed;         219 AA.
AC   P21974;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Probable deoxycytidine kinase FPV059;
DE            Short=dCK;
DE            EC=2.7.1.74;
GN   OrderedLocusNames=FPV059; ORFNames=FP26;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-1;
RX   PubMed=2165135; DOI=10.1099/0022-1317-71-7-1517;
RA   Tartaglia J., Winslow J., Goebel S.J., Johnson G.P., Taylor J.,
RA   Paoletti E.;
RT   "Nucleotide sequence analysis of a 10.5 kbp HindIII fragment of fowlpox
RT   virus: relatedness to the central portion of the vaccinia virus HindIII D
RT   region.";
RL   J. Gen. Virol. 71:1517-1524(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
RN   [3]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=8279127; DOI=10.1007/bf01702589;
RA   Koonin E.V., Senkevich T.G.;
RT   "Fowlpox virus encodes a protein related to human deoxycytidine kinase:
RT   further evidence for independent acquisition of genes for enzymes of
RT   nucleotide metabolism by different viruses.";
RL   Virus Genes 7:289-295(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a
CC         ribonucleoside 5'-diphosphate + dCMP + H(+); Xref=Rhea:RHEA:20061,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:57566,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=2.7.1.74;
CC   -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR   EMBL; X17202; CAA35067.1; -; Genomic_DNA.
DR   EMBL; AF198100; AAF44403.1; -; Genomic_DNA.
DR   PIR; D35216; D35216.
DR   RefSeq; NP_039022.1; NC_002188.1.
DR   SMR; P21974; -.
DR   PRIDE; P21974; -.
DR   GeneID; 1486607; -.
DR   KEGG; vg:1486607; -.
DR   Proteomes; UP000008597; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004137; F:deoxycytidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01673; dNK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR002624; DCK/DGK.
DR   InterPro; IPR031314; DNK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01712; dNK; 1.
DR   PIRSF; PIRSF000705; DNK; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..219
FT                   /note="Probable deoxycytidine kinase FPV059"
FT                   /id="PRO_0000175093"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         16..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   219 AA;  25909 MW;  4C3B08D885B58CE7 CRC64;
     MDSINEFTSK KLSIEGNISS GKTDVLNILR NINNVVSFHD VEDRYTPIEK ELIRKFHENP
     SRWSYALQTH YCMKRVRMHL ECFVPSRVNI LERSIFSDRY VFAEAATALG YMDDPEWALY
     CKQHDWYTDK LEIQFDGIIY LRTIPESCKE RINEKSITEK NYPNISIDYL KTLHEKHELW
     LTQCKKVPVL IIDGEEDFIF DPCAKKKLIN EVTEFINSI