ID   KITH_FOWPN              Reviewed;         183 AA.
AC   P10052;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   08-NOV-2023, entry version 96.
DE   RecName: Full=Thymidine kinase;
DE            EC=2.7.1.21;
GN   Name=TK; OrderedLocusNames=FPV086;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus; Fowlpox virus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3027984; DOI=10.1016/0042-6822(87)90415-6;
RA   Boyle D.B., Coupar B.E.H., Gibbs A.J., Seigman L.J., Both G.W.;
RT   "Fowlpox virus thymidine kinase: nucleotide sequence and relationships to
RT   other thymidine kinases.";
RL   Virology 156:355-365(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-9 / Isolate HP-440;
RX   PubMed=2838574; DOI=10.1099/0022-1317-69-6-1275;
RA   Binns M.M., Tomley F.M., Campbell J., Boursnell M.E.G.;
RT   "Comparison of a conserved region in fowlpox virus and vaccinia virus
RT   genomes and the translocation of the fowlpox virus thymidine kinase gene.";
RL   J. Gen. Virol. 69:1275-1283(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-9 / Isolate HP-440;
RX   PubMed=1326827; DOI=10.1016/0168-1702(92)90004-s;
RA   Binns M.M., Boursnell M.E.G., Skinner M.A.;
RT   "Gene translocations in poxviruses: the fowlpox virus thymidine kinase gene
RT   is flanked by 15 bp direct repeats and occupies the locus which in vaccinia
RT   virus is occupied by the ribonucleotide reductase large subunit gene.";
RL   Virus Res. 24:161-172(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Vaccine;
RA   Beisel C.E., Nazerian K.;
RL   Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Senthilvelan A., Purushothaman V., Palaniswami K.;
RT   "Sequence of thymidine kinase gene of Indian isolate of fowlpox virus.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M16617; AAA43822.1; -; Genomic_DNA.
DR   EMBL; D00321; BAA00233.1; -; Genomic_DNA.
DR   EMBL; AJ223385; CAA11295.1; -; Genomic_DNA.
DR   EMBL; X52860; CAA37041.1; -; Genomic_DNA.
DR   EMBL; AF198100; AAF44430.1; -; Genomic_DNA.
DR   EMBL; AF396867; AAK77606.1; -; Genomic_DNA.
DR   PIR; A27532; KIVZFP.
DR   RefSeq; NP_039049.1; NC_002188.1.
DR   SMR; P10052; -.
DR   GeneID; 1486634; -.
DR   KEGG; vg:1486634; -.
DR   Proteomes; UP000008597; Segment.
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; 3.30.60.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
DR   InterPro; IPR020633; Thymidine_kinase_CS.
DR   PANTHER; PTHR11441; THYMIDINE KINASE; 1.
DR   PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN           1..183
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000174930"
FT   ACT_SITE        89
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         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         163..167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   183 AA;  20381 MW;  FA60C5629F2DF276 CRC64;
     MSSGSIHVIT GPMFSGKTSE LVRRIKRFML SNFKCIIIKH CGDNRYNEDD INKVYTHDLL
     FMEATASSNL SVLVPTLLND GVQVIGIDEA QFFLDIVEFS ESMANLGKTV IVAALNGDFK
     RELFGNVYKL LSLAETVSSL TAICVKCYCD ASFSKRVTEN KEVMDIGGKD KYIAVCRKCF
     FSN
//