ID   KTHY_VACCW              Reviewed;         204 AA.
AC   Q80HT9; P13410;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=TMK; OrderedLocusNames=VACWR174; ORFNames=A48R;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2552411; DOI=10.1093/nar/17.19.7581;
RA   Smith G.L., de Carlos A., Chan Y.S.;
RT   "Vaccinia virus encodes a thymidylate kinase gene: sequence and
RT   transcriptional mapping.";
RL   Nucleic Acids Res. 17:7581-7590(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2045793; DOI=10.1099/0022-1317-72-6-1349;
RA   Smith G.L., Chan Y.S., Howard S.T.;
RT   "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the
RT   right inverted terminal repeat.";
RL   J. Gen. Virol. 72:1349-1376(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=1657913; DOI=10.1016/s0021-9258(18)54896-1;
RA   Hughes S.J., Johnston L.H., de Carlos A., Smith G.L.;
RT   "Vaccinia virus encodes an active thymidylate kinase that complements a
RT   cdc8 mutant of Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 266:20103-20109(1991).
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.
CC       {ECO:0000269|PubMed:1657913}.
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.
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO89453.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X16259; CAA34345.1; -; Genomic_DNA.
DR   EMBL; D11079; BAA01822.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89453.1; ALT_INIT; Genomic_DNA.
DR   PIR; E42522; KIVZ5W.
DR   SMR; Q80HT9; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000000344; 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   Reference proteome; Transferase.
FT   CHAIN           1..204
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_0000155219"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   204 AA;  23219 MW;  911DFD2C671CF6B3 CRC64;
     MSRGALIVFE GLDKSGKTTQ CMNIMESIPA NTIKYLNFPQ RSTVTGKMID DYLTRKKTYN
     DHIVNLLFCA NRWEFASFIQ EQLEQGITLI VDRYAFSGVA YAAAKGASMT LSKSYESGLP
     KPDLVIFLES GSKEINRNVG EEIYEDVTFQ QKVLQEYKKM IEEGDIHWQI ISSEFEEDVK
     KELIKNIVIE AIHTVTGPVG QLWM