ID J3U664_BACTU Unreviewed; 195 AA. AC J3U664; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 06-MAR-2013, entry version 5. DE RecName: Full=Thymidine kinase; DE EC=2.7.1.21; GN Name=tdk; ORFNames=BTG_21735; OS Bacillus thuringiensis HD-771. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1218175; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=HD-771; RA Doggett N., Teshima H., Bruce D., Detter J.C., Johnson S.L., Han C.; RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'- CC phosphate. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the thymidine kinase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP003752; AFQ17763.1; -; Genomic_DNA. DR RefSeq; YP_006605796.1; NC_018500.1. DR ProteinModelPortal; J3U664; -. DR GeneID; 13493061; -. DR KEGG; bti:BTG_21735; -. DR KO; K00857; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004797; F:thymidine kinase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR HAMAP; MF_00124; Thymidine_kinase; 1; -. DR InterPro; IPR001267; Thymidine_kinase. DR InterPro; IPR020633; Thymidine_kinase_CS. DR InterPro; IPR020634; Thymidine_kinase_subgr. DR PANTHER; PTHR11441; PTHR11441; 1. DR Pfam; PF00265; TK; 1. DR PIRSF; PIRSF035805; TK_cell; 1. DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding; KW Nucleotide-binding; Transferase; Zinc. FT NP_BIND 15 22 ATP (By similarity). FT NP_BIND 88 91 ATP (By similarity). FT ACT_SITE 89 89 Proton acceptor (By similarity). FT METAL 145 145 Zinc (By similarity). FT METAL 148 148 Zinc (By similarity). FT METAL 183 183 Zinc (By similarity). FT METAL 186 186 Zinc (By similarity). SQ SEQUENCE 195 AA; 21702 MW; 6B421C91EF8D86F4 CRC64; MYLINQNGWI EVICGSMFSG KSEELIRRVR RTQFAKQHAI VFKPCIDNRY SEEDVVSHNG LKVKAVPVSA SKDIFEHITE DMDVIAIDEV QFFDGDIVEV VQVLANRGYR VIVAGLDQDF RGLPFGQVPQ LMAIAEHVTK LQAVCSACGS PASRTQRLID GEPAAFDDPI ILVGASESYE PRCRHCHAVP TNKDK //