ID D1AP73_SEBTE Unreviewed; 357 AA. AC D1AP73; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAR-2024, entry version 73. 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=Sterm_3065 {ECO:0000313|EMBL:ACZ09907.1}; OS Sebaldella termitidis (strain ATCC 33386 / NCTC 11300). OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae; OC Sebaldella. OX NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ09907.1, ECO:0000313|Proteomes:UP000000845}; RN [1] {ECO:0000313|Proteomes:UP000000845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Mikhailova N., Sims D., Meincke L., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P., RA Woyke T., Wu D., Eisen J.A.; RT "The complete chromosome of Sebaldella termitidis ATCC 33386."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACZ09907.1, ECO:0000313|Proteomes:UP000000845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845}; RX PubMed=21304705; RA Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C., RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M., RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Beck B., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Chen F.; RT "Complete genome sequence of Sebaldella termitidis type strain RT (NCTC 11300)."; RL Stand. Genomic Sci. 2:220-227(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 -!- 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; CP001739; ACZ09907.1; -; Genomic_DNA. DR AlphaFoldDB; D1AP73; -. DR STRING; 526218.Sterm_3065; -. DR KEGG; str:Sterm_3065; -. DR eggNOG; COG0132; Bacteria. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_766818_0_0_0; -. DR Proteomes; UP000000845; 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; 2. 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; PF13500; AAA_26; 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; 2. 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:UP000000845}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}. FT ACT_SITE 95 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 17..24 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 94..97 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 151 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 154 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 189 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 192 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" SQ SEQUENCE 357 AA; 41102 MW; 05897B563B7A0BC5 CRC64; MNLYLSNNSG ILEVVTGSMF SGKSEELIRR LRRAKYAKQK TAVFKPAIDK RYEGDDVNIV SHSQNKIEAI LAKDVSVMEE YLENNPDIQV IGIDEAQFFG EDVVAFCEKC VKLGKRVVVA GLDMNFRGEP YEPMPRLMAT ADYVDKFHAI CTVCGNPAYV TQRIINGEPA YYDDPVLFVG TTESYEARCR RHHIVKYRDK KETKIYFVVG TDINVGKEHA ENEYIFENKN KQSMKILKIN NVEDVLDLAQ LRRDIKEATQ NHDVIVIRVI GGILYPLKEE YNLLNLMIEY RKESEVIVVA ENREGILNHV YLTIDVLHRN NINVKEVIYI NKNIENAEEA ANISRVSQRL KIPFRYL //