ID Q4CVY8_TRYCC Unreviewed; 415 AA. AC Q4CVY8; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 24-JAN-2024, entry version 76. DE RecName: Full=thymidine kinase {ECO:0000256|ARBA:ARBA00012118}; DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118}; GN ORFNames=Tc00.1047053511133.20 {ECO:0000313|EMBL:EAN84440.1}; OS Trypanosoma cruzi (strain CL Brener). OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum. OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN84440.1, ECO:0000313|Proteomes:UP000002296}; RN [1] {ECO:0000313|EMBL:EAN84440.1, ECO:0000313|Proteomes:UP000002296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN84440.1, RC ECO:0000313|Proteomes:UP000002296}; RX PubMed=16020725; DOI=10.1126/science.1112631; RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G., RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G., RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B., RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F., RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H., RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G., RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y., RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J., RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y., RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M., RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L., RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J., RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C., RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D., RA Andersson B.; RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas RT disease."; RL Science 309:409-415(2005). CC -!- SIMILARITY: Belongs to the thymidine kinase family. CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EAN84440.1}. 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; AAHK01001694; EAN84440.1; -; Genomic_DNA. DR RefSeq; XP_806291.1; XM_801198.1. DR AlphaFoldDB; Q4CVY8; -. DR SMR; Q4CVY8; -. DR STRING; 353153.Q4CVY8; -. DR PaxDb; 353153-Q4CVY8; -. DR EnsemblProtists; EAN84440; EAN84440; Tc00.1047053511133.20. DR GeneID; 3536254; -. DR KEGG; tcr:511133.20; -. DR eggNOG; KOG3125; Eukaryota. DR InParanoid; Q4CVY8; -. DR OrthoDB; 674053at2759; -. DR Proteomes; UP000002296; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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; 3.30.60.20; -; 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 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 {ECO:0000256|ARBA:ARBA00022840}; KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAN84440.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000002296}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAN84440.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 81..104 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT REGION 339..415 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 352..368 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 415 AA; 46347 MW; 0A6BD57D96723D13 CRC64; MCTLPSVGVC VCVCVRITFC SSRLGEEGKG REECLASSIA KVGCIVRVNY VLHLKKNEFY TPFLYLFVWV VDCTPTHRFT LLYLIFAFPP FFFFFIFFFF FVMFASHTST CTLKVHYAED QRNFRLAFGF CASSIQQLLA DTSLQMMLEN ESHGHIELII GPMFAGKTTE LMRRVRRELF ARRSCYVIKH SRDARYSRES VSSHDKLLLG ATAAVAELRE VGDAWCPYDV VAVDEGQFFP DIVAFCNTAA DAGKTVIVSA LDGDYRRQPF DGICRLIPLA ESVKKLTAVC MECHCRSASF TYRTVSSEKR ELIGGADMYI AACRTCFVTK SKKRAELEAK GSVQTPDKCS DTPAAEKQKG EQREAEEDPI TPPTTIAAAE PPLSASAVRK RPVGVDGNVP TDAERCTSKA RLECH //