ID   KTHY_CALMQ              Reviewed;         205 AA.
AC   A8MB58;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Probable thymidylate kinase {ECO:0000255|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000255|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000255|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000255|HAMAP-Rule:MF_00165}; OrderedLocusNames=Cmaq_0300;
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS   IC-167).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Caldivirga.
OX   NCBI_TaxID=397948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00165};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00165}.
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DR   EMBL; CP000852; ABW01148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8MB58; -.
DR   SMR; A8MB58; -.
DR   STRING; 397948.Cmaq_0300; -.
DR   EnsemblBacteria; ABW01148; ABW01148; Cmaq_0300.
DR   KEGG; cma:Cmaq_0300; -.
DR   eggNOG; arCOG01891; Archaea.
DR   HOGENOM; CLU_049131_1_3_2; -.
DR   OMA; VMTREPG; -.
DR   Proteomes; UP000001137; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 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..205
FT                   /note="Probable thymidylate kinase"
FT                   /id="PRO_1000123562"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   205 AA;  23286 MW;  4788C8D4BA919436 CRC64;
     MCIFVDVEGI DGVGKSTVIR LTADELRRRG YLVYTTSEPS DSPIGLFIRR SILESNLEVE
     PMALALLFAA DRVIHYNRVI KPKVKEGYIV ITERYIESSV AYQGSQGVPV EWIIEVNSMV
     AEPDLVIVLN APLNTVASRL SNRGMLEYFE RNTDFLRSVQ EVYLRRARER NYPVIDASRV
     INNVVNDVLT LIEDKAKGKC KNYNQ