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Database: UniProt
Entry: Q9JFB7
LinkDB: Q9JFB7
Original site: Q9JFB7 
ID   KITH_VACCT              Reviewed;         177 AA.
AC   Q9JFB7;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   05-DEC-2018, entry version 56.
DE   RecName: Full=Thymidine kinase;
DE            EC=2.7.1.21;
GN   Name=TK; ORFNames=TJ2R;
OS   Vaccinia virus (strain Tian Tan) (VACV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10253;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jin Q., Hou Y.D., Cheng N.H., Yao E.M., Cheng S.X., Yang X.K.,
RA   Jing D.Y., Yu W.H., Yuan J.S., Ma X.J.;
RT   "Complete genomic sequence of vaccinia virus (Tian Tan strain).";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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; AF095689; AAF33953.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9JFB7; -.
DR   Proteomes; UP000163220; 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    177       Thymidine kinase.
FT                                /FTId=PRO_0000174939.
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;  20118 MW;  480CE5FE6A3B3911 CRC64;
     MNGGHIQLMI GPMFSGKSTE LIRRVRRYQI AQYKCVTIKY SNDNRYGTGL WTHDKNNFEA
     LEATKLCDVL ESITDFSVIG IDEGQFFPDI VEFCERMANE GKIVIVAALD GTFQRKPFNN
     ILNLIPLSEM VVKLTAVCMK CFKEASFSKR LGEETEIEII GGNDMYQSVC RKCYIDS
//
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