ID Q06EL9_BPR32 Unreviewed; 193 AA.
AC Q06EL9;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 08-NOV-2023, entry version 73.
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};
GN Name=tk {ECO:0000313|EMBL:ABI94931.1};
GN ORFNames=RB32ORF107c {ECO:0000313|EMBL:ABI94931.1};
OS Escherichia phage RB32.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Straboviridae; Tevenvirinae; Tequatrovirus; Enterobacteria phage RB32.
OX NCBI_TaxID=2681602 {ECO:0000313|EMBL:ABI94931.1, ECO:0000313|Proteomes:UP000000912};
RN [1] {ECO:0000313|EMBL:ABI94931.1, ECO:0000313|Proteomes:UP000000912}
RP NUCLEOTIDE SEQUENCE.
RA Nolan J.M., Rowe R.D., Timpte C.S., Schluchter W.M.;
RT "Comparative analysis of close relatives of Bacteriophage T4.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ904452; ABI94931.1; -; Genomic_DNA.
DR RefSeq; YP_803049.1; NC_008515.1.
DR GeneID; 4405548; -.
DR KEGG; vg:4405548; -.
DR Proteomes; UP000000912; 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; 21610 MW; 83AE9A9C3FEAF403 CRC64;
MASLIFTYAA MNAGKSASLL TAAHNYKERG MSVLVLKPAI DTRDSVCEVV SRIGIKQEAN
IITDDMDIFE FYKWAEAQKD IHCVFVDEAQ FLKTEQVHQL SRIVDTYNVP VMAYGLRTDF
AGKLFEGSKE LLAIADKLIE LKAVCHCGKK AIMTARLMED GTPVKEGNQI CIGDEIYVSL
CRKHWNELTK KLG
//
