ID KITH_EHV1 Reviewed; 352 AA.
AC P69186; P09100; P28856;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 Equine herpesvirus 1 (strain HVS25A) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC Varicellovirus equidalpha1; Equid alphaherpesvirus 1.
OX NCBI_TaxID=10327;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2849761; DOI=10.1093/nar/16.23.11303;
RA Robertson G.R., Whalley J.M.;
RT "Evolution of the herpes thymidine kinase: identification and comparison of
RT the equine herpesvirus 1 thymidine kinase gene reveals similarity to a
RT cell-encoded thymidylate kinase.";
RL Nucleic Acids Res. 16:11303-11317(1988).
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; X13209; CAA31599.1; -; Genomic_DNA.
DR PIR; S01995; KIBED2.
DR RefSeq; YP_053084.1; NC_001491.2.
DR SMR; P69186; -.
DR GeneID; 1487533; -.
DR KEGG; vg:1487533; -.
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; P-loop containing nucleotide triphosphate hydrolases; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA synthesis; Early protein; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..352
FT /note="Thymidine kinase"
FT /id="PRO_0000175065"
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
//
