ID   Q38CF2_TRYB2            Unreviewed;       455 AA.
AC   Q38CF2;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=thymidine kinase {ECO:0000256|ARBA:ARBA00012118};
DE            EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118};
GN   ORFNames=Tb10.70.7270 {ECO:0000313|EMBL:EAN77518.1};
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431 {ECO:0000313|EMBL:EAN77518.1, ECO:0000313|Proteomes:UP000008524};
RN   [1] {ECO:0000313|EMBL:EAN77518.1, ECO:0000313|Proteomes:UP000008524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN77518.1,
RC   ECO:0000313|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA   Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA   Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA   Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA   Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA   Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA   Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA   Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA   Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA   Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA   Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA   Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA   Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA   Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA   Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA   Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
RN   [2] {ECO:0007829|PDB:5FUV, ECO:0007829|PDB:5FUW}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 203-384, AND DISULFIDE BONDS.
RX   PubMed=27426054; DOI=10.1111/MMI.13467;
RA   Valente M., Timm J., Castillo-Acosta V.M., Ruiz-Perez L.M., Balzarini T.,
RA   Nettleship J.E., Bird L.E., Rada H., Wilson K.S., Gonzalez-Pacanowska D.;
RT   "Cell cycle regulation and novel structural features of thymidine kinase,
RT   an essential enzyme in Trypanosoma brucei.";
RL   Mol. Microbiol. 102:365-385(2016).
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}.
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DR   EMBL; CM000208; EAN77518.1; -; Genomic_DNA.
DR   RefSeq; XP_822346.1; XM_817253.1.
DR   PDB; 5FUV; X-ray; 2.30 A; A/B=203-384.
DR   PDB; 5FUW; X-ray; 2.20 A; A/B=203-384.
DR   PDB; 5FUX; X-ray; 2.20 A; A/B=203-384.
DR   PDB; 5FUY; X-ray; 2.80 A; A/B/C/D/E/F=203-384.
DR   PDBsum; 5FUV; -.
DR   PDBsum; 5FUW; -.
DR   PDBsum; 5FUX; -.
DR   PDBsum; 5FUY; -.
DR   AlphaFoldDB; Q38CF2; -.
DR   SMR; Q38CF2; -.
DR   STRING; 185431.Q38CF2; -.
DR   PaxDb; 5691-EAN77518; -.
DR   GeneID; 3662841; -.
DR   KEGG; tbr:Tb10.70.7270; -.
DR   VEuPathDB; TriTrypDB:Tb927.10.880; -.
DR   eggNOG; KOG3125; Eukaryota.
DR   InParanoid; Q38CF2; -.
DR   OMA; HAQRSCY; -.
DR   OrthoDB; 674053at2759; -.
DR   Proteomes; UP000008524; Chromosome 10.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB.
DR   GO; GO:0005739; C:mitochondrion; ISM:GeneDB.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB.
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; IMP:GeneDB.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0015949; P:nucleobase-containing small molecule interconversion; ISM:GeneDB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010139; P:pyrimidine deoxyribonucleotide salvage; IMP:GeneDB.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IMP:GeneDB.
DR   GO; GO:0046104; P:thymidine metabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; 2.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 2.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5FUV, ECO:0007829|PDB:5FUW};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAN77518.1};
KW   Metal-binding {ECO:0007829|PDB:5FUV, ECO:0007829|PDB:5FUW};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAN77518.1};
KW   Zinc {ECO:0007829|PDB:5FUV, ECO:0007829|PDB:5FUW}.
FT   REGION          405..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:5FUX"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:5FUV, ECO:0007829|PDB:5FUW"
FT   BINDING         344
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:5FUV, ECO:0007829|PDB:5FUW"
FT   BINDING         374
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:5FUV, ECO:0007829|PDB:5FUW"
FT   BINDING         377
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:5FUV, ECO:0007829|PDB:5FUW"
FT   DISULFID        325
FT                   /note="Interchain"
FT                   /evidence="ECO:0007829|PDB:5FUV, ECO:0007829|PDB:5FUW"
SQ   SEQUENCE   455 AA;  50844 MW;  23B651D305F9BB8E CRC64;
     MHDGDGNIEL IIGPMFAGKT TELMRRVQRH KHAQRSCYII NYSRNSYQNQ RLSTHDQLSL
     TANVSIAKLS EVCDEWRDYD VIAVDNGQFF PDVVGFCARA ANEGKTVIVS ALDVDCRETP
     FDEVCRLVPR AESVLKLSAV CMECHEHDAF LTYRTIESNE RELYGGADMY LAVCRWCYKQ
     LTMSHVDAQK TSASTAAVVP NGAHGRIELI IGPMFAGKTT ELMRRVQRHK HAQRSCYIIK
     YTGDTRYSEG AITSHDQRAL TANVSVSNLH DVGDEWRKYD VIAVDEGQFF PGVAAFCSKA
     ADSGKVVIVS ALDADYLQEP FEEICLLVSR ADSVVKLSAV CMECHNRKAS FTYRTVKSDE
     RKLVGGSDMY MSVCRSCYET KRNMVQTEKY IYSCVGINEG SYSECSPGPS ERSSAGTSGV
     QTSVKVDEQN CTEPNTEAKK MPLKRKRNQM AVDTT
//