ID   KTHY_ECTVM              Reviewed;         204 AA.
AC   Q8JL72;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=TMK; OrderedLocusNames=EVM147;
OS   Ectromelia virus (strain Moscow) (ECTV) (Mousepox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=265874;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14675635; DOI=10.1016/s0042-6822(03)00520-8;
RA   Chen N., Danila M.I., Feng Z., Buller R.M., Wang C., Han X.,
RA   Lefkowitz E.J., Upton C.;
RT   "The genomic sequence of Ectromelia virus, the causative agent of
RT   mousepox.";
RL   Virology 317:165-186(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC         ChEBI:CHEBI:456216; EC=2.7.4.9;
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM92452.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF012825; AAM92452.1; ALT_INIT; Genomic_DNA.
DR   SMR; Q8JL72; -.
DR   UniPathway; UPA00575; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..204
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_0000155225"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   204 AA;  23291 MW;  BF1EDDDFA33A012A CRC64;
     MSRGALIVFE GLDKSGKTTQ CMNIMESIPS NTIKYLNFPQ RSTVTGKMID DYLTRKKTYN
     DHIVNLLFCA NRWEFASFIQ EQLEQGITLI VDRYAFSGVA YAAAKGAPMT LSKSYESGLP
     KPDLVIFLES GSKEINRNVG EEIYEDVEFQ QKVLQEYKKM IEEGDIHWQI ISSEFEEDVK
     KELIKNIVIE AMHTVTGPVG QLWM