ID   KITH_SHEVK              Reviewed;         177 AA.
AC   P16600;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Thymidine kinase;
DE            EC=2.7.1.21;
GN   Name=TK;
OS   Sheeppox virus (strain KS-1) (SPPV) (Capripoxvirus (strain KS-1)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Capripoxvirus.
OX   NCBI_TaxID=10269;
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2732700; DOI=10.1099/0022-1317-70-3-525;
RA   Gershon P.D., Black D.N.;
RT   "The nucleotide sequence around the capripoxvirus thymidine kinase gene
RT   reveals a gene shared specifically with leporipoxvirus.";
RL   J. Gen. Virol. 70:525-533(1989).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC   -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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DR   EMBL; D00423; BAA00324.1; -; Genomic_DNA.
DR   PIR; B31813; KIVZCP.
DR   SMR; P16600; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
DR   InterPro; IPR020633; Thymidine_kinase_CS.
DR   PANTHER; PTHR11441; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Transferase; Zinc.
FT   CHAIN           1..177
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000174929"
FT   ACT_SITE        83
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   177 AA;  20447 MW;  093E53E555F8E2C8 CRC64;
     MDYGYIHLII GPMFSGKSTE LIRIVKRYQI AQYKCCVVKY LKDIRYGNSV YTHDNNHVSA
     ISTTLLYDVV DKIMNFDIIG IDEGQFFKDI VSFSENMANM GKIIIIAALD STFQRKEFND
     ILKLIPLSEK VTKLNAVCME CYKDAAFSKR ITKEKEIELI GGKEKYKSVC RKCYFLE