ID KITH_RFVKA Reviewed; 178 AA. AC P07605; Q9Q910; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 14-DEC-2011, sequence version 2. DT 08-NOV-2023, entry version 81. DE RecName: Full=Thymidine kinase; DE EC=2.7.1.21; GN Name=TK; ORFNames=s061R; OS Rabbit fibroma virus (strain Kasza) (RFV) (Shope fibroma virus (strain OS Kasza)). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus; OC Rabbit fibroma virus. OX NCBI_TaxID=10272; OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3023681; DOI=10.1128/jvi.60.3.920-927.1986; RA Upton C., McFadden G.; RT "Identification and nucleotide sequence of the thymidine kinase gene of RT Shope fibroma virus."; RL J. Virol. 60:920-927(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3014722; DOI=10.1016/0042-6822(86)90134-0; RA Upton C., McFadden G.; RT "Tumorigenic poxviruses: analysis of viral DNA sequences implicated in the RT tumorigenicity of Shope fibroma virus and malignant rabbit virus."; RL Virology 152:308-321(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1660196; DOI=10.1016/0042-6822(91)90529-k; RA Strayer D.S., Jerng H.H., O'Connor K.; RT "Sequence and analysis of a portion of the genomes of Shope fibroma virus RT and malignant rabbit fibroma virus that is important for viral replication RT in lymphocytes."; RL Virology 185:585-595(1991). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10562495; DOI=10.1006/viro.1999.0002; RA Willer D.O., McFadden G., Evans D.H.; RT "The complete genome sequence of shope (Rabbit) fibroma virus."; RL Virology 264:319-343(1999). 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 -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}. 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; M14493; AAA47227.1; -; Genomic_DNA. DR EMBL; AF170722; AAF17943.1; -; Genomic_DNA. DR PIR; A26102; KIVZSF. DR RefSeq; NP_051950.1; NC_001266.1. DR SMR; P07605; -. DR GeneID; 1486904; -. DR KEGG; vg:1486904; -. DR Proteomes; UP000000868; Segment. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion 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: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 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 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. DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1. PE 3: Inferred from homology; KW ATP-binding; DNA synthesis; Kinase; Metal-binding; Nucleotide-binding; KW Reference proteome; Transferase; Zinc. FT CHAIN 1..178 FT /note="Thymidine kinase" FT /id="PRO_0000174935" FT ACT_SITE 85 FT /note="Proton acceptor" FT /evidence="ECO:0000255" FT BINDING 13..20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 115 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 143 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 159..163 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 172 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 175 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT CONFLICT 2..3 FT /note="Missing (in Ref. 1; AAA47227)" FT /evidence="ECO:0000305" FT CONFLICT 102 FT /note="A -> R (in Ref. 1; AAA47227)" FT /evidence="ECO:0000305" SQ SEQUENCE 178 AA; 19896 MW; 51A7775471A99D53 CRC64; MTMYGGHIHL IIGPMFAGKS TELIRLVRRY QIAKHKCLVV KYEKDIRYGN GVCTHDNMSI TAVCTPSLDK IDSVAENAEV IGIDEGQFFP NIATFCERMA NAGKVLIVAA LDGTFQRKPF SNISELIPLA ENVTKLNAVC MYCYKNGSFS KRLGDKMEIE VIGGSDKYKS VCRKCYFF //