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
//
