ID Q384A2_TRYB2 Unreviewed; 858 AA.
AC Q384A2;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 24-JAN-2024, entry version 125.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:EAN79879.1};
GN ORFNames=Tb11.01.1030 {ECO:0000313|EMBL:EAN79879.1};
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:EAN79879.1, ECO:0000313|Proteomes:UP000008524};
RN [1] {ECO:0000313|EMBL:EAN79879.1, ECO:0000313|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN79879.1,
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).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; CH464491; EAN79879.1; -; Genomic_DNA.
DR RefSeq; XP_828991.1; XM_823898.1.
DR AlphaFoldDB; Q384A2; -.
DR STRING; 185431.Q384A2; -.
DR PaxDb; 5691-EAN79879; -.
DR GeneID; 3664139; -.
DR KEGG; tbr:Tb11.01.1030; -.
DR VEuPathDB; TriTrypDB:Tb927.11.9270; -.
DR eggNOG; KOG0603; Eukaryota.
DR InParanoid; Q384A2; -.
DR OrthoDB; 163495at2759; -.
DR Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM:GeneDB.
DR GO; GO:0016301; F:kinase activity; IDA:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISM:GeneDB.
DR GO; GO:0044131; P:negative regulation of development of symbiont in host; IMP:GeneDB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:GeneDB.
DR GO; GO:0045926; P:negative regulation of growth; IMP:GeneDB.
DR GO; GO:0006468; P:protein phosphorylation; ISM:GeneDB.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd06093; PX_domain; 1.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024311; Lipocalin-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF234; SERINE/THREONINE-PROTEIN KINASE YPK2/YKR2; 1.
DR Pfam; PF13924; Lipocalin_5; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAN79879.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 30..154
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 264..314
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 363..617
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 201..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 858 AA; 96780 MW; 234FC71F56B61781 CRC64;
MLSKLFRYDT KLQGKQELST ADHRSLLELS MTDNITSVEI PQYRVRGTFV EYVIECTKRN
MTWQVFRRYQ QFKALDQSLK QLCSRGSSRH CDYGVIPVLC GSHWTEVTNQ SIDLVEKRRR
HLEIYLRQLL VPGNVFYVAK TVIYDFLHDG AVPAQHQRRA IRPLIGFATP DSLADLHLEN
RNGEGSASRL GAASTLNDKS ISMLGPSAVG ESDRVDDGVG DEEEEPCKSP PGETVESGEE
CEDLPSADNS EAEDVRVPPP GSLCRQCNAE FSSVLYPHRC FFCRQQFCRD CLHPVELEEG
EVARSCVQCY ENFARKTCKP QYPPTPMAST PILQCAPAGG ALDPLNLLGS TSHVRTDVTL
SDFKLVTTVG RGTFGKVMKV IFREDGKVYA MKVLNKCVIH KRRMIEYIRE EKNIMSSLPS
HPYIVTCHFA FQTDYHLFFV LDYLPGGDMH SRVYPKLKLT ESDVRLYIAE LVLALQHLHR
HDIAHRDVKL ENIVLGEDGH LKLTDFGLAR MNFSRQRRRS FVGSPEYLPP ETIQGKYQTK
AVDWWSAGVM LYEMLSGKTP FYSAYNCEIY NNVLKAELDL TAPCFTPEAA SLIEQLLQSH
PKARLQDAGA IKAHPYFASI DWAALEGKKI SAPIQLDLMG NDMKYIKWKF TAEWAVIYKP
PGVTRATIDL LINRFSNFAH VSEGTPPTPH LPIGQQQEEV SDGVTNPPDI TGVWNVVKVE
MQTEDGKITH PWGSAVCGVL AYFPEGQFSM QLTSYMRPHL RQQFVDRAVR EDLVEMCNSY
AGSFGKYQIK PGSNIITHRL HGCLCPNLTG STQKYFFEVR ERKENGAKVL KLFTACNALP
GEDISAQTVL TWERTGSC
//