ID C8ZBX6_YEAS8 Unreviewed; 2474 AA.
AC C8ZBX6;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=EC1118_1K5_0188g {ECO:0000313|EMBL:CAY80892.1};
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680 {ECO:0000313|EMBL:CAY80892.1, ECO:0000313|Proteomes:UP000000286};
RN [1] {ECO:0000313|EMBL:CAY80892.1, ECO:0000313|Proteomes:UP000000286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse
RC {ECO:0000313|Proteomes:UP000000286};
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambot B.,
RA Legras J.L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
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; FN393077; CAY80892.1; -; Genomic_DNA.
DR HOGENOM; CLU_000178_7_1_1; -.
DR Proteomes; UP000000286; Chromosome XI, Scaffold EC1118_1K5.
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:0035556; P:intracellular signal transduction; IEA:UniProt.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0019219; P:regulation of nucleobase-containing compound metabolic process; 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; 3.
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: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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 1338..1922
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2097..2421
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2442..2474
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2392..2419
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2474 AA; 281570 MW; 4C63D18666AB1526 CRC64;
MNKYINKYTT PPNLLSLRQR AEGKHRTRKK LTHKSHSHDD EMSTTSNTDS NHNGPNDSGR
VITGSAGHIG KISFVDSELD TTFSTLNLIF DKLKSDVPQE RASGANELST TLTSLAREVS
AEQFQRFSNS LNNKIFELIH GFTSSEKIGG ILAVDTLISF YLSTEELPNQ TSRLANYLRV
LIPSSDIEVM RLAANTLGRL AVPGGTLTSD FVEFEVRTCI DWLTLTADNN SSSSKLEYRR
HAALLIIKAL ADNSPYLLYA YVNSILDNIW VPLRDAKLII RLDAAVALGK CLTIIQDRDP
ALGKQWFQRL FQGCTHGLSL NTNDSVHATL LVFRELLSLK APYLRDKYDD IYKSTMKYKE
YKFDVIRREV YAILPLLAAF DPAIFTKKYL DRIMVHYLRY LKNIDMNAAN NSDKPFILVS
IGDIAFEVGS SISPYMTLIL DNIREGLRTK FKVRKQFEKD LFYCIGKLAC ALGPAFAKHL
NKDLLNLMLN CPMSDHMQET LMILNEKIPS LESTVNSRIL NLLSISLSGE KFIQSNQYDF
NNQFSIEKAR KSRNQSFMKK TGESNDDITD AQILIQCFKM LQLIHHQYSL TEFVRLITIS
YIEHEDPSVR KLAALTSCDL FIKDDICKQT SVHALHSVSE VLSKLLMIAI TDPVAEIRLE
ILQHLGSNFD PQLAQPDNLR LLFMALNDEI FGIQLEAIKI IGRLSSVNPA YVVPSLRKTL
LELLTQLKFS NMPKKKEESA TLLCTLINSS DEVAKPYIDP ILDVILPKCQ DASSAVASTA
LKVLGELSVV GGKEMTRYLK ELMPLIINTF QDQSNSFKRD AALTTLGQLA ASSGYVVGPL
LDYPELLGIL INILKTENNP HIRRGTVRLI GILGALDPYK HREIEVTSNS KSSVEQNAPS
IDIALLMQGV SPSNDEYYPT VVIHNLMKIL NDPSLSIHHT AAIQAIMHIF QNLGLRCVSF
LDQIIPGIIL VMRSCPPSQL DFYFQQLGSL ISIVKQHIRP HVEKIYGVIR EFFPIIKLQI
TIISVIESIS KALEGEFKRF VPETLTFFLD ILENDQSNKR IVSIRILKSL VTFGPNLEDY
SHLIMPIVVR MTEYSAGSLK KISIITLGRL AKNINLSEMS SRIVQALVRI LNNGDRELTK
ATMNTLSLLL LQLGTDFVVF VPVINKALLR NRIQHSVYDQ LVNKLLNNEC LPTNIIFDKE
NEVPERKNYE DEMQVTKLPV NQNILKNAWY CSQQKTKEDW QEWIRRLSIQ LLKESPSACL
RSCSSLVSVY YPLARELFNA SFSSCWVELQ TSYQEDLIQA LCKALSSSEN PPEIYQMLLN
LVEFMEHDDK PLPIPIHTLG KYAQKCHAFA KALHYKEVEF LEEPKNSTIE ALISINNQLH
QTDSAIGILK HAQQHNELQL KETWYEKLQR WEDALAAYNE KEAAGEDSVE VMMGKLRSLY
ALGEWEELSK LASEKWGTAK PEVKKAMAPL AAGAAWGLEQ WDEIAQYTSV MKSQSPDKEF
YDAILCLHRN NFKKAEVHIF NARDLLVTEL SALVNESYNR AYNVVVRAQI IAELEEIIKY
KKLPQNSDKR LTMRETWNTR LLGCQKNIDV WQRILRVRSL VIKPKEDAQV RIKFANLCRK
SGRMALAKKV LNTLLEETDD PDHPNTAKAS PPVVYAQLKY LWATGLQDEA LKQLINFTSR
MAHDLGLDPN NMIAQSVPQQ SKRVPRHVED YTKLLARCFL KQGEWRVCLQ PKWRLSNPDS
ILGSYLLATH FDNTWYKAWH NWALANFEVI SMLTSVSKKK QEGSDASSVT DINEFDNGMI
GVNTFDAKEV HYSSNLIHRH VIPAIKGFFH SISLSESSSL QDALRLLTLW FTFGGIPEAT
QAMHEGFNLI QIGTWLEVLP QLISRIHQPN QIVSRSLLSL LSDLGKAHPQ ALVYPLMVAI
KSESLSRQKA ALSIIEKMRI HSPVLVDQAE LVSHELIRMA VLWHEQWYEG LDDASRQFFG
EHNTEKMFAA LEPLYEMLKR GPETLREISF QNSFGRDLND AYEWLMNYKK SKDVSNLNQA
WDIYYNVFRK IGKQLPQLQT LELQHVSPKL LSAHDLELAV PGTRASGGKP IVKISKFEPV
FSVISSKQRP RKFCIKGSDG KDYKYVLKGH EDIRQDSLVM QLFGLVNTLL QNDAECFRRH
LDIQQYPAIP LSPKSGLLGW VPNSDTFHVL IREHREAKKI PLNIEHWVML QMAPDYDNLT
LLQKVEVFTY ALNNTEGQDL YKVLWLKSRS SETWLERRTT YTRSLAVMSM TGYILGLGDR
HPSNLMLDRI TGKVIHIDFG DCFEAAILRE KFPEKVPFRL TRMLTYAMEV SGIEGSFRIT
CENVMKVLRD NKDSLMAILE AFAFDPLINW GFDLPTKKIE EETGIQLPVM NANELLSNGA
ITEEEVQRVE NEHKNAIRNA RAMLVLKRIT DKLTGNDIRR FNDLDVPEQV DKLIQQATSV
ENLCQHYIGW CPFW
//
