ID E6SLB7_THEM7 Unreviewed; 266 AA. AC E6SLB7; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAR-2024, entry version 62. DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124}; DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124}; GN Name=tdk {ECO:0000256|HAMAP-Rule:MF_00124}; GN OrderedLocusNames=Tmar_1235 {ECO:0000313|EMBL:ADU51348.1}; OS Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM 10246 / OS 7p75a). OC Bacteria; Bacillota; Clostridia; Eubacteriales; OC Clostridiales Family XVII. Incertae Sedis; Thermaerobacter. OX NCBI_TaxID=644966 {ECO:0000313|EMBL:ADU51348.1, ECO:0000313|Proteomes:UP000008915}; RN [1] {ECO:0000313|EMBL:ADU51348.1, ECO:0000313|Proteomes:UP000008915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a RC {ECO:0000313|Proteomes:UP000008915}; RX PubMed=21304738; RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S., RA Del Rio T.G., Tice H., Cheng J.F., Tapia R., Goodwin L., Pitluck S., RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Schneider S., Rohde M., Goker M., Pukall R., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Detter J.C.; RT "Complete genome sequence of Thermaerobacter marianensis type strain RT (7p75a)."; RL Stand. Genomic Sci. 3:337-345(2010). RN [2] {ECO:0000313|Proteomes:UP000008915} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a RC {ECO:0000313|Proteomes:UP000008915}; RX DOI=10.4056/sigs.1373474; RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S., RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Schneider S., RA Rohde M., Goker M., Pukall R., Woyke T., Bristow J., Eisen J., RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Detter J.; RT "Complete genome sequence of Thermaerobacter marianensis type strain RT (7p75aT)."; RL Stand. Genomic Sci. 3:337-345(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00124, CC ECO:0000256|RuleBase:RU000544}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00124}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124}. CC -!- SIMILARITY: Belongs to the thymidine kinase family. CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|HAMAP-Rule:MF_00124, CC ECO:0000256|RuleBase:RU004165}. 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; CP002344; ADU51348.1; -; Genomic_DNA. DR AlphaFoldDB; E6SLB7; -. DR STRING; 644966.Tmar_1235; -. DR KEGG; tmr:Tmar_1235; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_3_0_9; -. DR Proteomes; UP000008915; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 3.30.60.20; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. 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; THYMIDINE KINASE; 1. DR PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1. DR Pfam; PF00265; TK; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00124}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124}; KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634, ECO:0000256|HAMAP- KW Rule:MF_00124}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00124}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00124}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00124}; Reference proteome {ECO:0000313|Proteomes:UP000008915}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}. FT REGION 187..266 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 87 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 10..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 86..89 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 143 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 146 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 181 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 184 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" SQ SEQUENCE 266 AA; 27344 MW; 41D81EF5FECC10B0 CRC64; MAGYLEVITG GMFSGKTEEL LRRVQRARIA RRQVLLCKPD LDHRYRRDAV ASHDGRDLQA AVVPAGRPEE LLALARAARA DVVGIDEAQF FAPGIVPTVL ELVAEGRRVI VSGLDMDFAR RPFGPMPELM AVADEVVKLK AICVVCGEPA TFTQRLIGGR PAAPDDPVIL IGGQESYEPR CRRHHQLAPG ENPARAQAAP AAPLAGPGAA RAAAGTAPAG AGASLAGSAW PAGGPAADPA GPSSPRTLGT PAGEGGSAPA GEEASP //