GenomeNet

Database: UniProt
Entry: B5Y8S5
LinkDB: B5Y8S5
Original site: B5Y8S5 
ID   KITH_COPPD              Reviewed;         198 AA.
AC   B5Y8S5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, 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=COPRO5265_0834;
OS   Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT).
OC   Bacteria; Coprothermobacterota; Coprothermobacteria;
OC   Coprothermobacterales; Coprothermobacteraceae; Coprothermobacter.
OX   NCBI_TaxID=309798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35245 / DSM 5265 / BT;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Coprothermobacter proteolyticus
RT   strain ATCC 5245 / DSM 5265 / BT.";
RL   Submitted (AUG-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; CP001145; ACI17535.1; -; Genomic_DNA.
DR   RefSeq; WP_012544187.1; NC_011295.1.
DR   ProteinModelPortal; B5Y8S5; -.
DR   SMR; B5Y8S5; -.
DR   STRING; 309798.COPRO5265_0834; -.
DR   EnsemblBacteria; ACI17535; ACI17535; COPRO5265_0834.
DR   KEGG; cpo:COPRO5265_0834; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; CAGLDQD; -.
DR   OrthoDB; 1279539at2; -.
DR   BioCyc; CPRO309798:G1GCO-793-MONOMER; -.
DR   Proteomes; UP000001732; 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    198       Thymidine kinase.
FT                                /FTId=PRO_1000095431.
FT   NP_BIND      15     22       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      87     90       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     88     88       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       144    144       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       147    147       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       182    182       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       185    185       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   198 AA;  21861 MW;  E89DD6D1AE8A97C6 CRC64;
     MEIITQDGWL EVITGCMFSG KTEELVRRLR RAVIAKKETI AIKPALDTRY DLVAVVSHSG
     FSFNAIPVED PKSILGMAKD AEVVGIDEAQ FFTGELVPVI RELLQNKKRV IVAGLDLDFR
     GEPFGIMPTL LALADEVTKL HAICSVCGNI ATKTQRLING RPARYDDPTI LVGGLETYEA
     RCNLHHEVPG KTLTLFKE
//
DBGET integrated database retrieval system