ID   KITH_BPT4               Reviewed;         193 AA.
AC   P13300;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   08-NOV-2023, entry version 99.
DE   RecName: Full=Thymidine kinase;
DE            EC=2.7.1.21;
GN   Name=TK;
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Straboviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3024113; DOI=10.1093/nar/14.21.8637;
RA   Valerie K., Stevens J., Lynch M., Henderson E.E., de Riel J.K.;
RT   "Nucleotide sequence and analysis of the 58.3 to 65.5-kb early region of
RT   bacteriophage T4.";
RL   Nucleic Acids Res. 14:8637-8654(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
CC   -!- FUNCTION: This thymidine kinase is one of the enzymes that catalyze DNA
CC       precursor synthesis. Although tk is a nonessential gene, some strains
CC       of host E.coli do not support the growth of phages that lack this gene.
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; X04567; CAA28234.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42663.1; -; Genomic_DNA.
DR   PIR; JF0016; KIBPT4.
DR   RefSeq; NP_049719.1; NC_000866.4.
DR   SMR; P13300; -.
DR   GeneID; 1258712; -.
DR   KEGG; vg:1258712; -.
DR   OrthoDB; 9611at10239; -.
DR   Proteomes; UP000009087; Segment.
DR   GO; GO:0005524; F:ATP 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   HAMAP; MF_00124; Thymidine_kinase; 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; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..193
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175058"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   193 AA;  21622 MW;  95D7BE1AEB9F2C49 CRC64;
     MASLIFTYAA MNAGKSASLL IAAHNYKERG MSVLVLKPAI DTRDSVCEVV SRIGIKQEAN
     IITDDMDIFE FYKWAEAQKD IHCVFVDEAQ FLKTEQVHQL SRIVDTYNVP VMAYGLRTDF
     AGKLFEGSKE LLAIADKLIE LKAVCHCGKK AIMTARLMED GTPVKEGNQI CIGDEIYVSL
     CRKHWNELTK KLG
//