ID   KITH_EHV1B              Reviewed;         352 AA.
AC   P69185; P09100; P28856;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
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}; OrderedLocusNames=38;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8387060; DOI=10.1016/0378-1119(93)90376-e;
RA   Corrochano L.M., Madueno F., Field H.J., de la Fuente R.;
RT   "Sequence analysis of thymidine kinase-defective mutants of equine
RT   herpesvirus-1 (EHV-1).";
RL   Gene 126:257-260(1993).
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}.
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; AY665713; AAT67296.1; -; Genomic_DNA.
DR   EMBL; X67961; CAA48144.1; -; Genomic_DNA.
DR   PIR; S01995; KIBED2.
DR   RefSeq; YP_053084.1; NC_001491.2.
DR   SMR; P69185; -.
DR   GeneID; 1487533; -.
DR   KEGG; vg:1487533; -.
DR   Proteomes; UP000001189; Genome.
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   Reference proteome; Transferase.
FT   CHAIN           1..352
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175066"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ   SEQUENCE   352 AA;  38750 MW;  66EF05158DD3B3F9 CRC64;
     MAARVPSGEA RRSASGAPVR RQVTIVRIYL DGVYGIGKST TGRVMASAAS GGSPTLYFPE
     PMAYWRTLFE ADVISGIYDT QNRKQQGDLA ADDAASITAH YQSRFTTPYL ILHDHTFGLF
     GGDSLQRGTR PDLTVVFDRH PVASAVCFPA ARYLIGDMSM CALIAMVATL PREPQGGNIV
     VTTLNVDEHV RRLRTRARIG EQIDMKLIAT LRNVYSMLAN TSNFLRSGRV WRDGWGELPL
     SCETYKHRAT QMDAFQERES PELSDTLFAM FKTPELLDDR GVILEVHAWA LDALMLKLRN
     LSVFCADLSG TPRQCAATVE SLIPLMSSTL SDSESASSLE RAARTFNAEM GV