ID   KITH_FHV1               Reviewed;         343 AA.
AC   P13159;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 85.
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   Feline herpesvirus 1 (FeHV-1) (Feline viral rhinotracheitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10334;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UC-D;
RX   PubMed=2746729; DOI=10.1128/jvi.63.8.3240-3249.1989;
RA   Nunberg J.H., Wright D.K., Cole G.E., Petrovskis E.A., Post L.E.,
RA   Compton T., Gilbert J.H.;
RT   "Identification of the thymidine kinase gene of feline herpesvirus: use of
RT   degenerate oligonucleotides in the polymerase chain reaction to isolate
RT   herpesvirus gene homologs.";
RL   J. Virol. 63:3240-3249(1989).
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   EMBL; M26660; AAA46172.1; -; Genomic_DNA.
DR   PIR; A32388; KIBEFH.
DR   RefSeq; YP_003331558.1; NC_013590.2.
DR   SMR; P13159; -.
DR   BindingDB; P13159; -.
DR   ChEMBL; CHEMBL1795128; -.
DR   DrugBank; DB03312; Brivudine.
DR   GeneID; 8658565; -.
DR   KEGG; vg:8658565; -.
DR   PRO; PR:P13159; -.
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..343
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175075"
FT   ACT_SITE        56
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         27..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ   SEQUENCE   343 AA;  38923 MW;  26B1A771E3AD1260 CRC64;
     MASGTIPVQN EEIIKSQVNT VRIYIDGAYG IGKSLTAKYL VRADENRPGY TYYFPEPMLY
     WRSLFETDVV GGIYAVQDRK RRGELSAEDA AYITAHYQAR FAAPYLLLHS RLSTITGYQK
     VVCEEHPDVT LIIDRHPLAS LVCFPLARYF VGDMTLGSVL SLMATLPREP PGGNLVVTTL
     NIEEHLKRLR GRSRTGEQID MKLIHALRNV YMMLVHTKKF LTKNTSWRDG WGKLKIFSHY
     ERNRLVETTI VSDSTESDLC DTLFSVFKAR ELSDQNGDLL DMHAWVLDGL METLQNLQIF
     TLNLEGTPDE CAAALGALRQ DMDMTFIAAC DMHRISEALT IYH