ID   KITH_MEHV1              Reviewed;         350 AA.
AC   P25987;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   24-JAN-2024, entry version 81.
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   Meleagrid herpesvirus 1 (MeHV-1) (Turkey herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Mardivirus;
OC   Mardivirus meleagridalpha1.
OX   NCBI_TaxID=37108;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
OH   NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2555435; DOI=10.1099/0022-1317-70-11-3055;
RA   Scott S.D., Ross N.L.J., Binns M.M.;
RT   "Nucleotide and predicted amino acid sequences of the Marek's disease virus
RT   and turkey herpesvirus thymidine kinase genes; comparison with thymidine
RT   kinase genes of other herpesviruses.";
RL   J. Gen. Virol. 70:3055-3065(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   RefSeq; NP_073316.1; NC_002641.1.
DR   SMR; P25987; -.
DR   GeneID; 918500; -.
DR   KEGG; vg:918500; -.
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..350
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175080"
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         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ   SEQUENCE   350 AA;  39968 MW;  AD3B8F96E431EB83 CRC64;
     MALPRRPPTL TRVYLDGPFG IGKTSILNAM PDHTPDGAPI LKVYEPMKYW RCQSTDLVVA
     ANETPERRRG GALSRFQSDM IMASIQARFA DPYLLFHERL SSKCRGKIEI CDTPAIILML
     DRHPVAAILC FPITRYLLGE YSLEMLISSI IRLPLESPGC NLTVTILPDE KEHVNRICSR
     DRPGETADRN MLRTLNAVYA SLVDTVKYAN LTCPYEKESW EMEWLGLPWF EESLLEEFIS
     RPRPVICSRT RMPLDRTLLA IFKRKELCSE NGELLTQYSW ILWGLLTKLH TINVELFDIS
     GMSRRECASA IMHTMPERLS TLASWNDLCE LEDDVISYNK GMCNEVGASR
//