ID G0X5N3_9CAUD Unreviewed; 193 AA.
AC G0X5N3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 22-FEB-2023, entry version 37.
DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00020079, ECO:0000256|RuleBase:RU000544};
DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
OS Escherichia phage wV7.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Straboviridae; Tevenvirinae; Tequatrovirus; Tequatrovirus vtec.
OX NCBI_TaxID=1054480 {ECO:0000313|EMBL:AEM00772.1, ECO:0000313|Proteomes:UP000000691};
RN [1] {ECO:0000313|EMBL:AEM00772.1, ECO:0000313|Proteomes:UP000000691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22923804; DOI=10.1128/JVI.01642-12;
RA Kropinski A.M., Lingohr E.J., Moyles D.M., Chibeu A., Mazzocco A.,
RA Franklin K., Villegas A., Ahmed R., She Y.M., Johnson R.P.;
RT "Escherichia coli O157:H7 Typing Phage V7 Is a T4-Like Virus.";
RL J. Virol. 86:10246-10246(2012).
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 Evidence={ECO:0000256|ARBA:ARBA00000506,
CC ECO:0000256|RuleBase:RU000544};
CC -!- SIMILARITY: Belongs to the thymidine kinase family.
CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}.
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DR EMBL; HM997020; AEM00772.1; -; Genomic_DNA.
DR RefSeq; YP_007004852.1; NC_019505.1.
DR GeneID; 14010646; -.
DR KEGG; vg:14010646; -.
DR Proteomes; UP000000691; Genome.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000544};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU000544};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000544};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000544};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT ACT_SITE 88
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ SEQUENCE 193 AA; 21638 MW; A453107302EAF41C CRC64;
MASLIFTYAA MNAGKSASLL TAAHNYKERG MSVLVLKPAI DTRDSVCEVV SRIGIRQEAN
IITDDMDIFE FYKWAEAQKD IHCVFVDEAQ FLKTEQVHQL SRIVDTYNVP VMAYGLRTDF
AGKLFEGSKE LLAIADKLIE LKAVCHCGKK AIMTARLMED GTPVKEGNQI CIGDEIYVSL
CRKHWNELTK KLG
//
