ID F9YU51_CAPCC Unreviewed; 239 AA. AC F9YU51; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 58. 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=Ccan_20530 {ECO:0000313|EMBL:AEK24169.1}; OS Capnocytophaga canimorsus (strain 5). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK24169.1, ECO:0000313|Proteomes:UP000008895}; RN [1] {ECO:0000313|EMBL:AEK24169.1, ECO:0000313|Proteomes:UP000008895} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895}; RX PubMed=21914877; DOI=10.1128/JB.05853-11; RA Manfredi P., Pagni M., Cornelis G.R.; RT "Complete genome sequence of the dog commensal and human pathogen RT Capnocytophaga canimorsus strain 5."; RL J. Bacteriol. 193:5558-5559(2011). 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00124}. 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; CP002113; AEK24169.1; -; Genomic_DNA. DR AlphaFoldDB; F9YU51; -. DR STRING; 860228.Ccan_20530; -. DR KEGG; ccm:Ccan_20530; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_3_0_10; -. DR Proteomes; UP000008895; 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: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 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. 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00124}; Reference proteome {ECO:0000313|Proteomes:UP000008895}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00124}. FT ACT_SITE 139 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 66..73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 138..141 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" SQ SEQUENCE 239 AA; 27104 MW; 7344888EC2AC8999 CRC64; MISKVFTNYI KNNKSLIYNT ILSLLVKNPS EIQKNTYFCE QYNSIMFLEN TTNYSEKFGW IEVICGSMFS GKTEELIRRL RRAQFAKQKV EIFKPAFDTR YDDVMVVSHN ANEIRSTPVP AAANIMLLAD GCDVIGIDEA QFFDDEIVTV CNDLANRGMR VIVAGLDMDF KGKPFGPMPA LMATAEYVTK VHAVCTRTGN LANFSYRKSA NENVFLLGEQ EAYEPLSRAA YFKAMKEKK //