ID I4EXF4_9ACTN Unreviewed; 240 AA. AC I4EXF4; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 24-JAN-2024, entry version 47. 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 Name=tdk {ECO:0000313|EMBL:CCH88067.1}; GN OrderedLocusNames=MODMU_2638 {ECO:0000313|EMBL:CCH88067.1}; OS Modestobacter marinus. OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales; OC Geodermatophilaceae; Modestobacter. OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH88067.1, ECO:0000313|Proteomes:UP000006461}; RN [1] {ECO:0000313|EMBL:CCH88067.1, ECO:0000313|Proteomes:UP000006461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC501 {ECO:0000313|EMBL:CCH88067.1, RC ECO:0000313|Proteomes:UP000006461}; RX PubMed=22887672; DOI=10.1128/JB.01029-12; RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L., RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A., RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.; RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501, RT a Representative Actinobacterium That Thrives on Calcareous Stone RT Surfaces."; RL J. Bacteriol. 194:4773-4774(2012). 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; FO203431; CCH88067.1; -; Genomic_DNA. DR RefSeq; WP_014740659.1; NC_017955.1. DR AlphaFoldDB; I4EXF4; -. DR STRING; 477641.MODMU_2638; -. DR KEGG; mmar:MODMU_2638; -. DR PATRIC; fig|477641.3.peg.2496; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_2_0_11; -. DR OMA; GTMDCGK; -. DR OrthoDB; 9781579at2; -. DR Proteomes; UP000006461; Chromosome. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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; 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:UP000006461}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}. FT ACT_SITE 109 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1" SQ SEQUENCE 240 AA; 26163 MW; 0166F4FEAD64C299 CRC64; MTPTPLLPDA VPASGDRRRH PAPAHLVFFH GPMDCGKSTL ALQVDHNQSR QGRHGLLLTQ GDRSGTPQIS SRVGLRREAV EVDPGTDVRL LVRDRWAGGH RVDYLIVDEA QFLTGEQVEQ LAELVDESHV DVYAFGLTTD FRARLFPGTQ RLFELADDVQ RVQVQVLCWC GLPGLLNARV VGGVMVREGA TVVVADTAPA AVPSAEAPGD DVRYQVLCRR HYVRGALEPT PTGPGQLALR //