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Database: UniProt
Entry: Q384A2_TRYB2
LinkDB: Q384A2_TRYB2
Original site: Q384A2_TRYB2 
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
//
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