ID   KTHY_VAR67              Reviewed;         205 AA.
AC   P0DSV5; P33803;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 8.
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 (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=587200;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1666548;
RA   Shchelkunov S.N., Marennikova S.S., Totmenin A.V., Blinov V.M.,
RA   Chizhikov V.E., Gutorov V.V., Safronov P.F., Pozdnyakov S.G.,
RA   Shelukhina E.M., Gashnikov P.V., Anjaparidze O.G., Sandakhchiev L.S.;
RT   "Creation of a clone library of fragments from the natural variola virus
RT   and study of the structural and functional organization of viral genes from
RT   a circle of hosts.";
RL   Dokl. Akad. Nauk SSSR 321:402-406(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA   Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT   "Genes of variola and vaccinia viruses necessary to overcome the host
RT   protective mechanisms.";
RL   FEBS Lett. 319:80-83(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X69198; CAA49101.1; -; Genomic_DNA.
DR   EMBL; X67118; CAA47543.1; -; Genomic_DNA.
DR   PIR; A36854; A36854.
DR   RefSeq; NP_042204.1; NC_001611.1.
DR   SMR; P0DSV5; -.
DR   GeneID; 1486448; -.
DR   KEGG; vg:1486448; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000002060; 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   Reference proteome; Transferase.
FT   CHAIN           1..205
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_0000155220"
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