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Database: UniProt
Entry: B1L989
LinkDB: B1L989
Original site: B1L989 
ID   KITH_THESQ              Reviewed;         184 AA.
AC   B1L989;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   16-JAN-2019, entry version 64.
DE   RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124};
DE            EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124};
GN   Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124};
GN   OrderedLocusNames=TRQ2_0533;
OS   Thermotoga sp. (strain RQ2).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=126740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RQ2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E.,
RA   Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P.,
RA   Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga sp. RQ2.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+);
CC         Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216;
CC         EC=2.7.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_00124};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00124}.
DR   EMBL; CP000969; ACB08887.1; -; Genomic_DNA.
DR   RefSeq; WP_012310602.1; NC_010483.1.
DR   ProteinModelPortal; B1L989; -.
DR   SMR; B1L989; -.
DR   EnsemblBacteria; ACB08887; ACB08887; TRQ2_0533.
DR   KEGG; trq:TRQ2_0533; -.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   OrthoDB; 1279539at2; -.
DR   BioCyc; TSP126740:G1GBG-549-MONOMER; -.
DR   Proteomes; UP000001687; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00124; Thymidine_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
DR   InterPro; IPR020633; Thymidine_kinase_CS.
DR   PANTHER; PTHR11441; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA synthesis; Kinase;
KW   Metal-binding; Nucleotide-binding; Transferase; Zinc.
FT   CHAIN         1    184       Thymidine kinase.
FT                                /FTId=PRO_1000095438.
FT   NP_BIND      10     17       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      83     86       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     84     84       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       140    140       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       143    143       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       173    173       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       176    176       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   184 AA;  20597 MW;  434A1E14C34C49D3 CRC64;
     MSGKLTVITG PMYSGKTTEL LSFVEIYKLG KKKVAVFKPK IDSRYHSTMI VSHSGNGVEA
     HVIERPEEMR KYIEEDTRGV FIDEVQFFSP GLFEVVKDLL DRGIDVFCAG LDLTHKQNPF
     ETTALLLSLA DTVIKKKAVC HRCGEYNATL TLKVAGGEEE IDVGGQEKYI AVCRDCYNTL
     KKRV
//
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