ID H8ZJN0_9PHYC Unreviewed; 176 AA. AC H8ZJN0; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 02-OCT-2024, entry version 29. DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544}; DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544}; GN ORFNames=OtV6_205c {ECO:0000313|EMBL:AFC35113.1}; OS Ostreococcus tauri virus RT-2011. OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes; OC Algavirales; Phycodnaviridae; Prasinovirus. OX NCBI_TaxID=1120767 {ECO:0000313|EMBL:AFC35113.1, ECO:0000313|Proteomes:UP000244668}; RN [1] {ECO:0000313|EMBL:AFC35113.1, ECO:0000313|Proteomes:UP000244668} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OtV6 {ECO:0000313|EMBL:AFC35113.1}; RA Thomas R., Derelle E., Cooke R., Moreau H.; RT "Circumventing host resistance to viruses: an Ostreococcus story."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. 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|RuleBase:RU000544}; CC -!- SIMILARITY: Belongs to the thymidine kinase family. CC {ECO:0000256|ARBA:ARBA00007587, 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; JN225873; AFC35113.1; -; Genomic_DNA. DR Proteomes; UP000244668; Genome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0046104; P:thymidine metabolic process; IEA:TreeGrafter. DR Gene3D; 3.30.60.20; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PIRSF; PIRSF035805; TK_cell; 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|RuleBase:RU000544}; KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634, KW ECO:0000256|RuleBase:RU000544}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000544}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000544}; KW Reference proteome {ECO:0000313|Proteomes:UP000244668}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}. FT ACT_SITE 83 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1" FT BINDING 168 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR035805-2" SQ SEQUENCE 176 AA; 19912 MW; 35F66DE3A08FBFBF CRC64; MSLSIIMGNM FSGKTSELIR RLKRLKILEK RIVVVNSAKD TRSPEQVLKT HDNVKFDCYK VLDLYELLNK DAFEDAEIVA IDEAQFFPNL KKFVECCLDM GKDVIIAGLD ADAFQRKWGE ILDCVPIACE VTKLSALCKY CRSGRPGPFT KRIVDNSDLE LIGGSDMYVA VCRKHL //