ID   KITH_SHV21              Reviewed;         527 AA.
AC   P21293;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   27-MAR-2024, entry version 97.
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   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Rhadinovirus;
OC   Rhadinovirus saimiriinegamma2; Saimiriine herpesvirus 2.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2555434; DOI=10.1099/0022-1317-70-11-3003;
RA   Honess R.W., Craxton M.A., Williams L., Gompels U.A.;
RT   "A comparative analysis of the sequence of the thymidine kinase gene of a
RT   gammaherpesvirus, herpesvirus saimiri.";
RL   J. Gen. Virol. 70:3003-3013(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(1992).
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; X64346; CAA45643.1; -; Genomic_DNA.
DR   EMBL; D00543; BAA00432.1; -; Genomic_DNA.
DR   RefSeq; NP_040223.1; NC_001350.1.
DR   GeneID; 1488261; -.
DR   KEGG; vg:1488261; -.
DR   Proteomes; UP000000587; Segment.
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; IPR013672; Herpes_TK_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10513; DEOXYNUCLEOSIDE KINASE; 1.
DR   PANTHER; PTHR10513:SF15; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 10, MITOCHONDRIAL; 1.
DR   Pfam; PF00693; Herpes_TK; 1.
DR   Pfam; PF08465; Herpes_TK_C; 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   Reference proteome; Transferase.
FT   CHAIN           1..527
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175077"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        243
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         216..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         368
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         374
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ   SEQUENCE   527 AA;  59807 MW;  4E8E3A3A178FAD7D CRC64;
     MTGRGQPPKK NDTYDYPRKQ PPKNGSYDNY DYPTSTKTRS TNKQRKDSNY PPRETIFEPD
     LAADPIYSVP RPPSRVPHKL VKVNYKSNLV PITASNSVSE LLSLHDETQV TECVEAPLIA
     KSPDITVYEK MFSVRPKHTL TKLEGKQKMF TRKKKGSFVK IGSNMLEFGE SLKSKLHNDS
     KKSPDEPDGL VHVPVHLLYP PKHQDPVPAF FIFLEGSIGV GKTTLLKSMN GILGGKNVLA
     FHEPIAYWTD VFSNSLEEVY KLTLPAKVGR TSNSAKLLAC QLKFASPLLA LKTATDRLSS
     PKNSLLSSDM WVMFDRHPLS ATVVFPYMHF QNGFLSFSHL IQLWSSFKAS RGDNIILLNL
     NSQENLKRVK KRNRKEEKSV SIEHIRLLNN CYHAVYCAWL LVQNFTPEEI VEVCFNAKHI
     TDLSSSKPSF LAKHVSTEDM LKSSIFNTWI EMTKAHRDSC TLMECLLTFC KELEKVQLIH
     VNVSPFTDDI PGLWASIYTS IRRNSAIKPN RVNWLALEDL ARTFNSQ
//