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Database: UniProt
Entry: P10052
LinkDB: P10052
Original site: P10052 
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   16-JAN-2019, entry version 85.
DE   RecName: Full=Thymidine kinase;
DE            EC=2.7.1.21;
GN   Name=TK; OrderedLocusNames=FPV086;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Avipoxvirus.
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
RT   to 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
RT   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
RT   gene is flanked by 15 bp direct repeats and occupies the locus which
RT   in vaccinia virus is occupied by the ribonucleotide reductase large
RT   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
RT   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(+);
CC         Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216;
CC         EC=2.7.1.21;
CC   -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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   ProteinModelPortal; P10052; -.
DR   SMR; P10052; -.
DR   GeneID; 1486634; -.
DR   KEGG; vg:1486634; -.
DR   Proteomes; UP000008597; Genome.
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   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; Complete proteome; DNA synthesis; Kinase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT   CHAIN         1    183       Thymidine kinase.
FT                                /FTId=PRO_0000174930.
FT   NP_BIND      11     18       ATP. {ECO:0000250}.
FT   REGION      163    167       Substrate binding. {ECO:0000250}.
FT   ACT_SITE     89     89       Proton acceptor. {ECO:0000255}.
FT   METAL       144    144       Zinc. {ECO:0000250}.
FT   METAL       147    147       Zinc. {ECO:0000250}.
FT   METAL       176    176       Zinc. {ECO:0000250}.
FT   METAL       179    179       Zinc. {ECO:0000250}.
FT   BINDING     119    119       Substrate; via amide nitrogen.
FT                                {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
//
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