ID D0A3T9_TRYB9 Unreviewed; 2432 AA.
AC D0A3T9;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=TbgDal_X10260 {ECO:0000313|EMBL:CBH15933.1};
OS Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH15933.1, ECO:0000313|Proteomes:UP000002316};
RN [1] {ECO:0000313|Proteomes:UP000002316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA Barry J.D., Berriman M., Hertz-Fowler C.;
RT "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT chronic human african trypanosomiasis.";
RL PLoS Negl. Trop. Dis. 4:E658-E658(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC ECO:0000256|RuleBase:RU364109};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031, ECO:0000256|RuleBase:RU364109}.
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DR EMBL; FN554973; CBH15933.1; -; Genomic_DNA.
DR RefSeq; XP_011778197.1; XM_011779895.1.
DR GeneID; 23864194; -.
DR KEGG; tbg:TbgDal_X10260; -.
DR VEuPathDB; TriTrypDB:Tbg972.10.10260; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000002316; Chromosome 10.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024585; mTOR_dom.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR_cat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF115; SERINE_THREONINE-PROTEIN KINASE TOR; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364109};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364109};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364109}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU364109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT DOMAIN 1286..1848
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2032..2344
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2400..2432
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2432 AA; 271444 MW; E9928DFC866B9E65 CRC64;
MEGCAHPLTS QLQPIFSELH SGKLATLSST ISKLENVLKD QGDGFFQSNS ECQSREANLR
LSVWISSQIG QLFRRPETQR AAILCVKTLL DVEYEAINNL DQTFLRLLED SVKCADMSVS
RMAAEVWGLW LNNSGTSTEG IAQSRLKICF ADLRESDKVM DKVAACLFLE ELLKRTPSTV
APLLDVVAEC LHPAVLSSSD LVQASAATAL RYVLLLMYTS MNPSGIKKWY ETFLSASLDA
LRSGAPERRT GAIRCFNAVM SSVTSNVSAC DTAVTFSETS VAHVHEIWEY VSEQVTLTST
LELRRELLQS LTILALYDTE AFKRMSIAKV VEAASGVFQT PAEKDLEPLV FQTLGKLAGV
MPDQIVTFLG CSMHHIEEVL KQGRHDACGL GAIACVAAFA EVNPRAVRPY LRQILAPILS
GSLTVDFAKG VARICAAFPE LRSTCLSKIL EVAKKQLRDD RCNAGGAGAL CDGGVSPEAQ
ILSALSNLEF AGYPTLPFLC DTAVAYVSVP NGEVRRAAIK LCFKLVLSGC LGPQSPCRQT
SDGVVIHSGC EHTQLFNKVI KKLVNAAVAD PESDIRLDTL RNFTEEFDHT LALRDVVRSL
FPALHDKHQN RLAVVRLLGR VSRRNPAHVY PMLRRIMVQC VTEMQYFEHA KKQEQAFSVL
GAIIESAPGL CKPYISSLLN MCAARLSDGT READVCAALL SCVGKLVRYA EGDDIRVCAR
IRPIVVQHIL DSSHLPKKRE ALRALGDIVR TTKDVNVYED HAELLPVLLQ ALHGGFKELW
PVRKDVLQLM GIIGAVDPVR VKEILRGPRV NNNTKLVPFL PFEGEDTIAQ TVVRSVLHIL
SLPSLTEDQS VAAVQVIVGI FSLEVLSPGC LVSFYGEVIS SIQKQARVQV RKREEILVHL
ISLVRILKGH LRPHLKEITS TVDSFISAID LSVLRQVLAL LKELCCSLRE EFRPYMSSLL
GPIIVLVEEN VEETSEIVLD FFSAMGSLLE DHLHTVLPVV CNIIVDTSVP SRCRIVAVKT
LICFTKRLPD LCFHASRCVH CLCRVLRESD GGDGVGDEGR LGCSAMEALC TLAGSLGKNF
ENFVLVVLPA VADRYGETSG EYCRFCHDIY EAIDGKRAPE VSSNGVGKAG GGGAPSLPFT
AGTSASPLKD RADAYASLRF HLRKRDQASD EDWNHWLPQL AVNLLRSSSS PSHGRALTLA
ELHEPFARQM LHSAFAACYA DMDEHTQREV IGLLTEVLRG LRVPSEVMQE LLNLSEHMER
QGIRLSAGGK ASIKHSSNFC PFDRQVLMES SANCNLYSKA LHYAEIEFFE TVREYERSIL
RGCPKPLPVE DWQNLIKLCE KSIYFCNLLG QRESANGILK FIRQNLPLLT GKKVTELSQM
MDAHLFDKLR WWSQSLQAYE RRLQQEPNKV SNMVGLLRAL DALGEYPRVL EMWRQFSKRV
SKREVSKLAS MGAHAAWLLR RWDDMEHITS FMSDEDYTGT TALFYKATLA ARKKRFREAE
KLIDMCRKRV DSKLSALVAE SYDRAYDLFV GIQQLSELEE LAMATSDPQS AMHWRQLWER
RLSVMAYEGW PGTLANHTLL VPPSSEIDMW LRFVSLSRAH GQGSVSTEVL RELLGNQSIE
SAIENGIPTP AVAMGSFQHL YETNQRDSAI ARLQLYVSKV EGSGAQHVSR EREDMAVCHA
KLAEWLVHQK KAHRTEDELQ KIFHHLRRAT ELDKSNGSIW RTLARVHREA ATKPADGSDS
SGASGHIMEA LSAYLRSVSL SEELEDALGF LSLWFMYGPL LAVQVGSTLK EEIEEVNPTV
WLKVIPQIIA RISSPNGTVA DSVYNLLVLV ARRHPQAILY SLNVAHSSYQ GKGTADGVEP
LKGSHRVLAR IAEIHQNGKA MVEDSALVCR ELVRCAVLWP ELWINELGRA LYQWERQRSA
ENLLLAMGPL LEQLKRPETM AEAQFAAELR QPLENACCHV ERAVSSRHEQ FMEEARRIFV
SIERRIREQI SGMSSLALQL VSPKLHQNGR NLSLVVPGQY REDGNYPLIA SFQNVLKVLN
SKQRPRRIYI NGSNGEIYKF LLKGHEDLRL DERVMQLLGF VNTILEKHSV AKRHDCLIQT
YSVTPLSDNA GLVGWVDHCD TLNKIIEDYR VNPRCIRMEL DLMRSMCDNL YYLTAIQRVE
PFEFALERTE GVDLVRSFWV KAPSAETWLE RRTTYVCSLA TMSMVGHILG LGDRHPSNLM
IHAFSGRVVH IDFGDCFEVA QQRSIHPEKV PFRLTRMLVK AMEMGGIEGL FRHGCHTVMN
VLREEGGSLL ALLEAFVHDP LVSWWRDEAE GFSGNGQTAS SVQTISVIGS MTNVAEEGSV
GSLQLSQLSV QRRATTQQRV NANIEKDTSQ TRKPKSVVKR IKRKLRGLEF PQSQEGKSSD
GFTVEEQVSR LIEEATSNEN LCVHFLGWCP FW
//
