ID   KITH_SHV1               Reviewed;         361 AA.
AC   P04408;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   24-JAN-2024, entry version 85.
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   Saimiriine herpesvirus 1 (strain MV-5-4-PSL) (SaHV-1) (Marmoset
OS   herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus saimiriinealpha1.
OX   NCBI_TaxID=10353;
OH   NCBI_TaxID=9481; Callithrix.
OH   NCBI_TaxID=9520; Saimiri (squirrel monkeys).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6330976; DOI=10.1016/0042-6822(84)90189-2;
RA   Otsuka H., Kit S.;
RT   "Nucleotide sequence of the marmoset herpesvirus thymidine kinase gene and
RT   predicted amino acid sequence of thymidine kinase polypeptide.";
RL   Virology 135:316-330(1984).
RN   [2]
RP   SEQUENCE REVISION.
RA   Kit S.;
RL   Submitted (JUN-1989) 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; K02122; AAA67102.1; -; Genomic_DNA.
DR   PIR; A00614; KIBETM.
DR   SMR; P04408; -.
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   CDD; cd02019; NK; 1.
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..361
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175078"
FT   ACT_SITE        46
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         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ   SEQUENCE   361 AA;  39458 MW;  B2E322DB1D5542DB CRC64;
     MSGTAGTSRI LRVYLDGPHG VGKSTTAEAL VARCEPRRPI RSMLQEPMAY WRSTFASDAI
     TEIYDTQHRL DSNEITAAEA GAFMTSLQLH MGTPYALLEE AMRPHVGREL AEPDDNGPLP
     QRRDFVLVVD RHAVASMVCY PLARFMMGCV SLRSVASLIS HLPPPLPGTN LVVASLDFRE
     HAARLRARAR PGERLDLTMM AAIRNAYAML ANTSRYLLSG GDWRRDWGSL PVFKPSAFVA
     RAAKTAYTLP LRDEPGLADT LFAALKVPEF LDARGYPRAA HAWTLDILAN RIRALRVYTL
     DLTGPPEACA AAFRRLCAGL VLTEGSHPGA LCELKRAAAA YAREMSVVGS REPTTAEVES
     A
//