ID   KITH_ILTVT              Reviewed;         364 AA.
AC   P23983;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Infectious laryngotracheitis virus (strain Thorne V882) (ILTV) (Gallid
OS   herpesvirus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX   NCBI_TaxID=10344;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2157797; DOI=10.1099/0022-1317-71-4-841;
RA   Griffin A.M., Boursnell M.E.;
RT   "Analysis of the nucleotide sequence of DNA from the region of the
RT   thymidine kinase gene of infectious laryngotracheitis virus; potential
RT   evolutionary relationships between the herpesvirus subfamilies.";
RL   J. Gen. Virol. 71:841-850(1990).
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; D00565; BAA00442.1; -; Genomic_DNA.
DR   PIR; D43675; D43675.
DR   RefSeq; YP_182352.1; NC_006623.1.
DR   SMR; P23983; -.
DR   GeneID; 3239035; -.
DR   KEGG; vg:3239035; -.
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..364
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175081"
FT   ACT_SITE        64
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ   SEQUENCE   364 AA;  40215 MW;  C1C04A7342ECCF7E CRC64;
     MAVAGAVKTS GGVQFCSEFE NDDSDFRRVV LLYVDGPFGV GKTVTAKTLM QMPNWRGCRL
     YLAEPMQAWR QWFGGADMIK EINEIQTLKA SGKLECREAS PVAVAEVQMT IAAPLRIMNH
     VIYNYLGSER CYSAAASGPD DVLFLVDRHP LAACLCFPVA QYLSGALEFG DLITLLSGIP
     DIPTHSNIVL MDLDICEQAR RIIQRGRPGE TVDWTYLCAL RNSYICLMNT TTYLQRTSYP
     ALLKEQEALT SATLLKFKRE CLETATVPEI NPSIDQTLFA ILAFDQQNVH GERLKTVLSF
     VVQKLATVLK NLCIFYLPAH GLTPEACALK CLEFAETASS LTTKRAAIAS LIDAVERYNA
     DMGS