ID   KITH_HHV8P              Reviewed;         580 AA.
AC   F5HB62;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 35.
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=ORF21;
OS   Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS   sarcoma-associated herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=868565;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA   Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT   "Identification of a spliced gene from Kaposi's sarcoma-associated
RT   herpesvirus encoding a protein with similarities to latent membrane
RT   proteins 1 and 2A of Epstein-Barr virus.";
RL   J. Virol. 73:6953-6963(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA   Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT   "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL   J. Gen. Virol. 87:1781-1804(2006).
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; AF148805; ABD28872.1; -; Genomic_DNA.
DR   RefSeq; YP_001129374.1; NC_009333.1.
DR   BioGRID; 1776987; 37.
DR   PRIDE; F5HB62; -.
DR   DNASU; 4961484; -.
DR   GeneID; 4961484; -.
DR   KEGG; vg:4961484; -.
DR   Proteomes; UP000000942; Genome.
DR   GO; GO:0019033; C:viral tegument; IDA:CACAO.
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..580
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000423759"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..149
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         260..267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         421
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ   SEQUENCE   580 AA;  64537 MW;  C34E41D6B181DAFB CRC64;
     MAEGGFGADS VGRGGEKASV TRGGRWDLGS SDDESSTSTT STDMDDLPEE RKPLTGKSVK
     TSYIYDVPTV PTSKPWHLMH DNSLYATPRF PPRPLIRHPS EKGSIFASRL SATDDDSGDY
     APMDRFAFQS PRVCGRPPLP PPNHPPPATR PADASMGDVG WADLQGLKRT PKGFLKTSTK
     GGSLKARGRD VGDRLRDGGF AFSPRGVKSA IGQNIKSWLG IGESSATAVP VTTQLMVPVH
     LIRTPVTVDY RNVYLLYLEG VMGVGKSTLV NAVCGILPQE RVTSFPEPMV YWTRAFTDCY
     KEISHLMKSG KAGDPLTSAK IYSCQNKFSL PFRTNATAIL RMMQPWNVGG GSGRGTHWCV
     FDRHLLSPAV VFPLMHLKHG RLSFDHFFQL LSIFRATEGD VVAILTLSSA ESLRRVRARG
     RKNDGTVEQN YIRELAWAYH AVYCSWIMLQ YITVEQMVQL CVQTTNIPEI CFRSVRLAHK
     EETLKNLHEQ SMLPMITGVL DPVRHHPVVI ELCFCFFTEL RKLQFIVADA DKFHDDVCGL
     WTEIYRQILS NPAIKPRAIN WPALESQSKA VNHLEETCRV