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Database: UniProt
Entry: P68564
LinkDB: P68564
Original site: P68564 
ID   KITH_VACCC              Reviewed;         177 AA.
AC   P68564; P03297;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   13-FEB-2019, entry version 49.
DE   RecName: Full=Thymidine kinase;
DE            EC=2.7.1.21;
GN   Name=TK; ORFNames=J2R;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   COMPLETE GENOME.
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
CC   -!- FUNCTION: Phosphorylates thymidine and thymidine analogs, such as
CC       azidothymidine (AZT). Part of the salvage pathway for pyrimidine
CC       deoxyribonucleotide synthesis (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Homotetramer. Two molecules of substrate bind to each
CC       enzyme tetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
DR   EMBL; M35027; AAA48082.1; -; Genomic_DNA.
DR   PIR; A00609; KIVZ.
DR   ProteinModelPortal; P68564; -.
DR   Proteomes; UP000008269; 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; Transferase; Zinc.
FT   CHAIN         1    177       Thymidine kinase.
FT                                /FTId=PRO_0000174938.
FT   NP_BIND      11     18       ATP. {ECO:0000250}.
FT   REGION      157    161       Substrate binding. {ECO:0000250}.
FT   ACT_SITE     83     83       Proton acceptor. {ECO:0000255}.
FT   METAL       138    138       Zinc. {ECO:0000250}.
FT   METAL       141    141       Zinc. {ECO:0000250}.
FT   METAL       170    170       Zinc. {ECO:0000250}.
FT   METAL       173    173       Zinc. {ECO:0000250}.
FT   BINDING     113    113       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
SQ   SEQUENCE   177 AA;  20100 MW;  57E3595EBE6F3C54 CRC64;
     MNGGHIQLII GPMFSGKSTE LIRRVRRYQI AQYKCVTIKY SNDNRYGTGL WTHDKNNFEA
     LEATKLCDVL ESITDFSVIG IDEGQFFPDI VEFCERMANE GKIVIVAALD GTFQRKPFNN
     ILNLIPLSEM VVKLTAVCMK CFKEASFSKR LGEETEIEII GGNDMYQSVC RKCYIDS
//
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