ID KITH_EHV4 Reviewed; 352 AA. AC P24425; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 24-JAN-2024, entry version 99. DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_04029}; DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_04029}; GN Name=TK {ECO:0000255|HAMAP-Rule:MF_04029}; OS Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus; OC Varicellovirus equidalpha4; Equid alphaherpesvirus 4. OX NCBI_TaxID=10333; OH NCBI_TaxID=9796; Equus caballus (Horse). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2391500; DOI=10.1099/0022-1317-71-8-1801; RA Nicolson L., Cullinane A.A., Onions D.E.; RT "The nucleotide sequence of the equine herpesvirus 4 thymidine kinase RT gene."; RL J. Gen. Virol. 71:1801-1805(1990). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-352 IN COMPLEXES WITH RP THYMIDINE; ADP AND BISUBSTRATE ANALOGS, ACTIVE SITE, CATALYTIC ACTIVITY, RP AND SUBUNIT. RX PubMed=14527394; DOI=10.1016/j.str.2003.09.003; RA Gardberg A., Shuvalova L., Monnerjahn C., Konrad M., Lavie A.; RT "Structural basis for the dual thymidine and thymidylate kinase activity of RT herpes thymidine kinases."; RL Structure 11:1265-1277(2003). CC -!- FUNCTION: Catalyzes the transfer of the gamma-phospho group of ATP to CC thymidine to generate dTMP in the salvage pathway of pyrimidine CC synthesis. The dTMP serves as a substrate for DNA polymerase during CC viral DNA replication. Allows the virus to be reactivated and to grow CC in non-proliferative cells lacking a high concentration of CC phosphorylated nucleic acid precursors. {ECO:0000255|HAMAP- CC Rule:MF_04029}. 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:0000255|HAMAP-Rule:MF_04029, CC ECO:0000269|PubMed:14527394}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_04029, CC ECO:0000269|PubMed:14527394}. CC -!- SIMILARITY: Belongs to the herpesviridae thymidine kinase family. CC {ECO:0000255|HAMAP-Rule:MF_04029}. 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; D14486; BAA03378.1; -; Genomic_DNA. DR PIR; A36657; KIBEE4. DR PDB; 1P6X; X-ray; 2.00 A; A/B=23-352. DR PDB; 1P72; X-ray; 2.10 A; A/B=23-352. DR PDB; 1P73; X-ray; 2.70 A; A/B/C/D=23-352. DR PDB; 1P75; X-ray; 3.02 A; A/B/C/D=23-352. DR PDBsum; 1P6X; -. DR PDBsum; 1P72; -. DR PDBsum; 1P73; -. DR PDBsum; 1P75; -. DR SMR; P24425; -. DR DrugBank; DB03280; p1-(5'-adenosyl)p5-(5'-thymidyl)pentaphosphate. DR DrugBank; DB04485; Thymidine. DR EvolutionaryTrace; P24425; -. 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-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006230; P:TMP biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_04029; HSV_KITH; 1. DR InterPro; IPR001889; Herpes_TK. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00693; Herpes_TK; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; DNA synthesis; Early protein; Kinase; KW Nucleotide-binding; Transferase. FT CHAIN 1..352 FT /note="Thymidine kinase" FT /id="PRO_0000175067" FT ACT_SITE 60 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029" FT BINDING 32..39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029, FT ECO:0000269|PubMed:14527394, ECO:0007744|PDB:1P72" FT BINDING 78 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029, FT ECO:0000269|PubMed:14527394, ECO:0007744|PDB:1P72" FT BINDING 102 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029, FT ECO:0000269|PubMed:14527394, ECO:0007744|PDB:1P72" FT BINDING 105 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:14527394, FT ECO:0007744|PDB:1P72" FT BINDING 148 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:14527394, FT ECO:0007744|PDB:1P72" FT BINDING 192 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029, FT ECO:0000269|PubMed:14527394, ECO:0007744|PDB:1P72" FT BINDING 198 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04029" FT STRAND 23..31 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 38..46 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:1P6X" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 62..66 FT /evidence="ECO:0007829|PDB:1P6X" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 73..86 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 91..117 FT /evidence="ECO:0007829|PDB:1P6X" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:1P6X" FT STRAND 132..139 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 142..145 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 147..154 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 160..167 FT /evidence="ECO:0007829|PDB:1P6X" FT STRAND 177..183 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 186..196 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 205..226 FT /evidence="ECO:0007829|PDB:1P6X" FT TURN 231..237 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 243..249 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 263..265 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 267..271 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 285..298 FT /evidence="ECO:0007829|PDB:1P6X" FT STRAND 301..307 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 312..320 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 321..325 FT /evidence="ECO:0007829|PDB:1P6X" FT STRAND 328..332 FT /evidence="ECO:0007829|PDB:1P6X" FT HELIX 333..350 FT /evidence="ECO:0007829|PDB:1P6X" SQ SEQUENCE 352 AA; 38784 MW; F925ACF592077456 CRC64; MAACVPPGEA PRSASGTPTR RQVTIVRIYL DGVYGIGKST TGRVMASAAS GGSPTLYFPE PMAYWRTLFE TDVISGIYDT QNRKQQGNLA VDDAALITAH YQSRFTTPYL ILHDHTCTLF GGNSLQRGTQ PDLTLVFDRH PVASTVCFPA ARYLLGDMSM CALMAMVATL PREPQGGNIV VTTLNVEEHI RRLRTRARIG EQIDITLIAT LRNVYFMLVN TCHFLRSGRV WRDGWGELPT SCGAYKHRAT QMDAFQERVS PELGDTLFAL FKTQELLDDR GVILEVHAWA LDALMLKLRN LNVFSADLSG TPRQCAAVVE SLLPLMSSTL SDFDSASALE RAARTFNAEM GV //