ID   Q4E1S0_TRYCC            Unreviewed;       355 AA.
AC   Q4E1S0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=thymidine kinase {ECO:0000256|ARBA:ARBA00012118};
DE            EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118};
GN   ORFNames=Tc00.1047053506855.260 {ECO:0000313|EMBL:EAN98732.1};
OS   Trypanosoma cruzi (strain CL Brener).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN98732.1, ECO:0000313|Proteomes:UP000002296};
RN   [1] {ECO:0000313|EMBL:EAN98732.1, ECO:0000313|Proteomes:UP000002296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL Brener {ECO:0000313|EMBL:EAN98732.1,
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:EAN98732.1}.
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DR   EMBL; AAHK01000044; EAN98732.1; -; Genomic_DNA.
DR   RefSeq; XP_820583.1; XM_815490.1.
DR   AlphaFoldDB; Q4E1S0; -.
DR   SMR; Q4E1S0; -.
DR   STRING; 353153.Q4E1S0; -.
DR   PaxDb; 353153-Q4E1S0; -.
DR   EnsemblProtists; EAN98732; EAN98732; Tc00.1047053506855.260.
DR   GeneID; 3553296; -.
DR   KEGG; tcr:506855.260; -.
DR   eggNOG; KOG3125; Eukaryota.
DR   InParanoid; Q4E1S0; -.
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:EAN98732.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002296};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAN98732.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..355
FT                   /note="thymidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004237434"
FT   TRANSMEM        27..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          281..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   355 AA;  39745 MW;  E698AEE10A76400E CRC64;
     MNFTLFFLFL LVWVVDCTPT HRFTLLYLIF AFPPFLFVVV VVMFASHTST CTLKLRYAED
     QRNFRLAFGF CASSIQQLFA DISLQMMLEN ESHGHIELII GPMFAGKTTE LMRRVRRELF
     AKRSCYVIKH SRDARYSRES VSSHDKLLLG ATAAVAELRE VGDAWRPFDV VAVDEGQFFP
     DIVGFCNTAA DAGKTVIVSA LDGDYRRQPF DGICRLIPLA ESVKKLTAVC MECHCRSASF
     TYRTVSSEKR ELIGGADMYI AACRTCFVTK SKKRAEMEAK GSVQTVDKCS DTPAAEKQKG
     EQREVEEDPI TPPTTIAAAE TPLSASAARK RPVDVDENVP TDAERCKSKA RLECH
//