ID   KITH_EHV2               Reviewed;         613 AA.
AC   Q66624;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 2.
DT   03-AUG-2022, entry version 70.
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=21;
OS   Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX   NCBI_TaxID=82831;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA   Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus 2.";
RL   J. Mol. Biol. 249:520-528(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   Davison A.J.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; U20824; AAC13808.2; -; Genomic_DNA.
DR   PIR; S55615; S55615.
DR   RefSeq; NP_042617.2; NC_001650.2.
DR   GeneID; 1461018; -.
DR   KEGG; vg:1461018; -.
DR   Proteomes; UP000007083; 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; IPR013672; Herpes_TK_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00693; Herpes_TK; 1.
DR   Pfam; PF08465; Herpes_TK_C; 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..613
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000405986"
FT   REGION          1..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         301..308
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         461
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ   SEQUENCE   613 AA;  68665 MW;  406E210129510171 CRC64;
     MAEGGAGFSS SSTSSEEAVP WSTQQPMGWE ELESLGDGGG STSADEEFQW EAMFVKSRAG
     SPTAEDKSRT FTLPRGRPKN EPRPERGKGK TPKKPKKPDQ GATLLVGEEP RPRLGSRTRS
     KSRSRDKHQL PDDIYDVPNP PMLAPVDSYG NPVEQVSSSE SDFEDIANIR PILRRQQPVT
     VKHRREPSPE PLGHPTFVHR YDKPSYDEEV CQKKDKGGRT KSKNWLRQPG VKSKLTSMKD
     LSGSFKSLMH IRSDGEKHKQ QQRPGGSGAP GGATPRDVFN TFLGSGTCPS FKNAFFLYLE
     GSMGVGKTTL IRHMREINGD NVISFVEPMF YWREVYSDCV KLIYSACKPF NLGKMSTSNK
     VLSAQMKFMT PMKCLQTSVR RYVKANEPLQ EKTAMDNWLL FDRHPLSATL VFPYLSLKNG
     YLAFEHFLAL AANFTAHEGD IIALLCMGEE DNLKMVKLRN RKGESGVTSA HLKDLGQAFH
     ACYCTWLLLK YLSPEDMVSV CCCDVTLNDI CIMRSMSSSK VTMAKSLFNK SMFPTLMDVI
     QPFRSNCTII EICLTLFMEL KKVEFIVVNA SEFIGDIPGV WTSIYTQSLR TQAIKTQSID
     WSGLRAFSLT YNS