ID   KTHY_CAMPM              Reviewed;         204 AA.
AC   Q8V2K9;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=TMK; OrderedLocusNames=CMLV169;
OS   Camelpox virus (strain M-96).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=203173;
OH   NCBI_TaxID=9836; Camelus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12033760; DOI=10.1006/viro.2001.1343;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Sandybaev N.T., Kerembekova U.Z.,
RA   Zaitsev V.L., Kutish G.F., Rock D.L.;
RT   "The genome of camelpox virus.";
RL   Virology 295:1-9(2002).
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=AAL73876.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF438165; AAL73876.1; ALT_INIT; Genomic_DNA.
DR   SMR; Q8V2K9; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000152221; Genome.
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_0000155221"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   204 AA;  23237 MW;  6C15E537543CA180 CRC64;
     MSRGALIVFE GLDKSGKTTQ CMNIMESILA NTIKYLNFPQ RSTVTGKMID DYLTRKKTYN
     DHIVNLLFCA NRWEFASFIQ EQLEQGITLI VDRYAFSGVA YAAAKGASMT LSKSYEFGLP
     KPDLVIFLES GSKEINKNVG EEIYEDVAFQ QKVLQEYKKM IEEGDIHWQI ISSEFEEDVK
     KELIKNIVIE AIHTVTGPVG QLWM