ID   KITH_BHV1Q              Reviewed;         359 AA.
AC   P24424;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_04029};
DE            EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_04029};
GN   Name=TK {ECO:0000255|HAMAP-Rule:MF_04029};
OS   Bovine herpesvirus 1.2 (strain Q3932) (BoHV-1) (Infectious bovine
OS   rhinotracheitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10321;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2172455; DOI=10.1099/0022-1317-71-10-2417;
RA   Smith G.A., Young P.L., Mattick J.S.;
RT   "The location and nucleotide sequence of the thymidine kinase gene of
RT   bovine herpesvirus type 1.2.";
RL   J. Gen. Virol. 71:2417-2424(1990).
CC   -!- FUNCTION: Catalyzes the transfer of the gamma-phospho group of ATP to
CC       thymidine to generate dTMP in the salvage pathway of pyrimidine
CC       synthesis. The dTMP serves as a substrate for DNA polymerase during
CC       viral DNA replication. Allows the virus to be reactivated and to grow
CC       in non-proliferative cells lacking a high concentration of
CC       phosphorylated nucleic acid precursors. {ECO:0000255|HAMAP-
CC       Rule:MF_04029}.
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:0000255|HAMAP-Rule:MF_04029};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_04029}.
CC   -!- SIMILARITY: Belongs to the herpesviridae thymidine kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_04029}.
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DR   PIR; A36254; KIBEBT.
DR   SMR; P24424; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006230; P:TMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_04029; HSV_KITH; 1.
DR   InterPro; IPR001889; Herpes_TK.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00693; Herpes_TK; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA synthesis; Early protein; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..359
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175062"
FT   ACT_SITE        45
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         17..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ   SEQUENCE   359 AA;  36903 MW;  C3DB4930FB300025 CRC64;
     MAEPARALRV VRIYLDGAHG LGKTTTGRAL AAASTAGEGV LFFPEPMAYW RTMFVTDALS
     GILAASARCA AASHGSARGA GGPAHRADAD AAGLVAYYQA RFAAPYLILH ARVSALLAPP
     GPAPGGTVTL VFDRHPVAAC LCYPFARYCL REINAEDLLM LAAAMPPEAP GANLVVCTLP
     PAEQQRRLAA RARPGDRADA GFLVAVRNAY ALLVNTCAFL RAGGAWRDGW DALEWADANA
     LAALADPSCD ECKMAPAPAL RDTLFAALKC RELYPGGGAG LPAVHAWALD ALAGRLAALE
     VFVLDVSAAP DACAAAVLDM RPAMQAACAD GAAGATLATL ARQFALEMAG EATAGPRGL