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Database: UniProt
Entry: C1D0Z6
LinkDB: C1D0Z6
Original site: C1D0Z6 
ID   KITH_DEIDV              Reviewed;         202 AA.
AC   C1D0Z6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   16-JAN-2019, entry version 53.
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=Deide_06660;
OS   Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCD115 / DSM 17065 / LMG 22923;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P.,
RA   Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P.,
RA   Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S.,
RA   Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of
RT   Sahara bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO45520.1; -; Genomic_DNA.
DR   RefSeq; WP_012692643.1; NC_012526.1.
DR   ProteinModelPortal; C1D0Z6; -.
DR   SMR; C1D0Z6; -.
DR   STRING; 546414.Deide_06660; -.
DR   PaxDb; C1D0Z6; -.
DR   PRIDE; C1D0Z6; -.
DR   EnsemblBacteria; ACO45520; ACO45520; Deide_06660.
DR   KEGG; ddr:Deide_06660; -.
DR   eggNOG; ENOG4107T8J; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   OrthoDB; 1279539at2; -.
DR   BioCyc; DDES546414:G1GCG-781-MONOMER; -.
DR   Proteomes; UP000002208; 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; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    202       Thymidine kinase.
FT                                /FTId=PRO_1000203110.
FT   NP_BIND      16     23       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      99    102       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE    100    100       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       156    156       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       159    159       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       194    194       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       197    197       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   202 AA;  21720 MW;  EE884E842CB25251 CRC64;
     MLKSPYSGGH LEVIVGPMFS GKSEELIRRV TRALIARQRV QVFKPAVDDR YHESAVASHA
     GRTVGALAVG DVADIRAHLS GEAPLLQASA EMPDVIGIDE VQFFGPELVP LALELADAGV
     RVILAGLDLD FRAEPFGCMP DLLARAESVE KLTAICTQCG APATRSQRLI SGEPARFDDP
     VVLVGALESY EARCRLHHVV TR
//
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