ID A0A0F7RYJ2_9BASI Unreviewed; 1630 AA.
AC A0A0F7RYJ2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN Name=SSCI41980.1 {ECO:0000313|EMBL:CDS00383.1};
OS Sporisorium scitamineum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=49012 {ECO:0000313|EMBL:CDS00383.1, ECO:0000313|Proteomes:UP000242770};
RN [1] {ECO:0000313|Proteomes:UP000242770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman P.J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; CCFA01002509; CDS00383.1; -; Genomic_DNA.
DR STRING; 49012.A0A0F7RYJ2; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000242770; Unassembled WGS sequence.
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; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic 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 PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 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; 1.
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; PS00915; PI3_4_KINASE_1; 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|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU364109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT DOMAIN 472..1027
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1203..1516
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1598..1630
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 1630 AA; 183421 MW; C6A9A66D25B208EF CRC64;
MGILGALDPY RYKLLEKNGD EGQDETSKGS GTDLFELALA IGTSTDDYYQ NIAIDALITI
LKDPSLSTHH HAVIEAVMYM FKTQGLKCVT FLPQIIPAFL NVIRTCGTGL SEFYFQQLAI
LISIIKQHVR SYLEPIFELV QENWNPNSSI QLTIVSLVEA VAKALEGEFK SYLPILLPNM
LQTLDGEITS KRQPTLLRIL QAFYVFGSNI EEYLHLVLPV VVKMFERPDA SQTLRRAAIL
TVGNLSRKVS FCDHASRIIH PLVRVLPTGT SDIRNAVMET LSALVVQLGA SYAIFIPVVN
KVLVQNRIQH ATYDQLVTKL LNGERLPQDL SSADNALGSK IDESPQAEAN KMTVNQQHLK
QAWDTSKVST SEDWQEWLRR MAVEFMRESP SHALRACRSL ADVYPALAYG LFNVAFVSCW
TELYEQYQSD LVKALETAFD APEVPGDVVH MLLNLAEFME HDDKALPINI RVLGDRAYKF
HSYAKALHYK EAEFLTDPSP QVVESLIDIN TKLQQSDAAF GALTYAREHL DITHHEEWYE
KLHRWEEALA AYDRKAMLDP DDYAVAFGKM RCLHALGEWE HLSDLVQQKW GRADMEDRRH
MAPLAAAAAW SLGQWDSMDD YISAMRSDSS ERSFYRAILH THRSQRAAAN KQIAKARESL
DSELTALISE SYGRAYDLMV RTQMLSELEE ALAYKLDYKE QPDRQATIRS TWMKRLKGCQ
PEVEVWQRIL SVRSIVLTPA DDTETWIKFA NLCRKSGRMV LAEKTLNSLL GPERTNADPR
SLIGPRAPPP VIYAHLKFMW ASGARIESLS YLQEFTLNLA EDLGAHTVDE HDNLVTQDWQ
SSPRLGEFAR LLARCFFKQG EWQISLRENW VTDDNSNVIE SYRRATELDR NWYKAWHAWA
LANFEIISHH EERNEQITPQ MIAASIVPSV QGFFRSIALA SGNSLQDTLR LLTLWFKYGH
QEDVSQAVSE GFASVIVDTW LEVIPQIIAR ITAPSPRVRR LIHNLLSDVG LAHPQALVYP
LTVAAKSPSH MRIQAAMGIM DNVREHSPVL VEQALLVSNE LIRVAILWHE MWHEGLEEAS
RLYFTEHNID AMFATLEPLH DALEKGPETM RETSFSQSHG RDLAEARECG RRFRQYGDIS
DLNQAWDLYY HVFKKITKQL PAGNSVQLDL QHVSPKLLAM RDLELAVPGT YQSGKPIVCI
TRFEQMVLVI ASKQHPRRLK MKGSDGKTYQ YLLKGHEDLR QDERVMQLFG LVNTLLSIDS
ESYKRRLEIR RFPVIPLSPN TGMLGWVENT DTLHVLIKEY REQHKILLNI EHRLMLQMAP
DYDHLTLMQK VEVFEYALDN TPGQDLYRVL WLKSRNSESW LERRLAYTRS LAVSSVAGYI
LGLGDRHPSN LLLDRLTGQI VHIDFGDCFE IACHRPKFPE KVPFRLTRML VNAMEVGGIK
GTFKVTAENT MRVLRDNKES VLALLEAFVH DPLISWRLVA DDAEQQRAPD AQENEAAAVG
AGNTAAATNA GEGAVTGAAN VGAAGTVAPN QRQEASQAGT AAGAGAATGG AIAAPGGGAA
AAGGAPGAAG QDMRNQRALE VVRRIQNKLS GRDFNPAESL SVSAQIERLV QDATSKENLC
VAFVGWCSFW
//
