ID   KITH_AHV1W              Reviewed;         686 AA.
AC   P33802;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 70.
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}; Synonyms=BXLF1;
OS   Alcelaphine herpesvirus 1 (strain WC11) (AlHV-1) (Malignant catarrhal fever
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX   NCBI_TaxID=33705;
OH   NCBI_TaxID=59528; Connochaetes gnou (Black wildebeest).
OH   NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2167059; DOI=10.1007/bf01318352;
RA   Hsu D., Shih L.M., Zee Y.C.;
RT   "Nucleotide sequence of a 3.5 kilobase fragment of malignant catarrhal
RT   fever virus strain WC11.";
RL   Arch. Virol. 113:53-60(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   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   Transferase.
FT   CHAIN           1..686
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175060"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        270
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         243..250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         398
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
FT   BINDING         404
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04029"
SQ   SEQUENCE   686 AA;  77074 MW;  06A817D080826A5F CRC64;
     MASNSHNNYN TPRRQNYDVP KAWEEDSLYE NIDFLTQPAV SSDTSEDEEP LLSVARRVEV
     QGVNPGLKPR GLVRPRQDAD NPSSDEGFDW ELWKLHLSTR AFSFLEPPRL SSSNTASGLR
     SSCSDFTILG SSGVNPTSHA NLSEEEMYEE IPPLASNPSD ERHPRQLSGA VAQGAIRKSP
     RKLKFKPAKF KGLSSSLLNP FTASDSGRRA RRQTPTCQPG FTPIFQDLGE PHYVKACTVF
     FEGCMAAGKT TLLNFARQTL SDDEALTIPE PMRFWTEVYT NVLSQIVKIN KECKPGKTST
     TAELVSCQLK FATPLKTQSL FLQRSVKKDS EMQPVGPLDK WVIVDRHQLS ALVVFPLVLM
     RRGMLSFSDF FNLLGMFEAH PGEVIALMSV NVEENFTRLK KRGRVCERHI DRDYIKEIKG
     SFNAAYCAWL FLQYFSIQTT MQICMGLSSL DEACATEGVC HTTASRIWNN RMLVTLSDII
     SQFSNDYTVQ NVCYNFFSQL STLKFVVIDL SAFRHDVPGA WGEFYMQVMK NGDIKTRVMD
     FTAIKALADT AHNTHLRSIS FSSSQVFSTM LFLILLCVTG AQAITTPAPP RPATTTPRRG
     VTSAPLIVPA SSSELIVTLD GTFHSVTIDM TEIRQYVRQE IIEALWNASH VFESLETTYN
     RYKDVYRFTD QSIRVNTRGS CQLVKK