ID   KTHY_VARV               Reviewed;         205 AA.
AC   P0DSV6; P33803;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=TMK; ORFNames=A48R, J2R;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Harvey;
RX   PubMed=1331292; DOI=10.1099/0022-1317-73-11-2887;
RA   Aguado B., Selmes I.P., Smith G.L.;
RT   "Nucleotide sequence of 21.8 kbp of variola major virus strain Harvey and
RT   comparison with vaccinia virus.";
RL   J. Gen. Virol. 73:2887-2902(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
CC   -!- FUNCTION: Poxvirus TMP kinase is able to phosphorylate dTMP, dUMP and
CC       also dGMP from any purine and pyrimidine nucleoside triphosphate. The
CC       large substrate specificity is explained by the presence of a canal
CC       connecting the edge of the dimer interface to the TMP base binding
CC       pocket, canal not found in the human homolog (By similarity).
CC       {ECO:0000250}.
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   -!- SUBUNIT: Homodimer; the dimer arrangement is orthogonal and not
CC       antiparallel as in human enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR   EMBL; L22579; AAA60903.1; -; Genomic_DNA.
DR   PIR; G72170; G72170.
DR   PIR; JQ1855; JQ1855.
DR   RefSeq; NP_042204.1; NC_001611.1.
DR   SMR; P0DSV6; -.
DR   GeneID; 1486448; -.
DR   KEGG; vg:1486448; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000119805; 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; 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..205
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_0000448111"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   205 AA;  23378 MW;  59E603FA7AB92566 CRC64;
     MSRGALIVFE GLDKSGKTTQ CMNIMESIPT NTIKYLNFPQ RSTVTGKMID DYLTRKKTYN
     DHIVNLLFCA NRWEFASFIQ EQLEQGITLI VDRYAFSGVA YATAKGASMT LSKSYESGLP
     KPDLVIFLES GSKEINRNVG EEIYEDVAFQ QKVLQEYKKM IEEGEDIHWQ IISSEFEEDV
     KKELIKNIVI EAIHTVTGPV GQLWM