ID A0A067NI32_PLEOS Unreviewed; 2663 AA.
AC A0A067NI32;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=PLEOSDRAFT_1113153 {ECO:0000313|EMBL:KDQ26640.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ26640.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031, ECO:0000256|RuleBase:RU364109}.
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DR EMBL; KL198009; KDQ26640.1; -; Genomic_DNA.
DR STRING; 1137138.A0A067NI32; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1113153; -.
DR HOGENOM; CLU_000178_7_1_1; -.
DR InParanoid; A0A067NI32; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000027073; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR032805; Wax_synthase_dom.
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; PF13813; MBOAT_2; 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 SUPFAM; SSF48452; TPR-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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364109};
KW Reference proteome {ECO:0000313|Proteomes:UP000027073};
KW 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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1559..2100
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2274..2588
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2631..2663
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2663 AA; 299984 MW; BC81AB9E2CDD6A8E CRC64;
MAGMLFSTLQ SLGLVPGVTY LVTAVGVLLP SRILRTSAFL VNLVIVYHSI RSTATNVPAH
DYSVGSGYIT LLIHSSVLLL LSSPRSDFRQ LNQAEPTTTL SWLQWAFALL TSPRLIGWTT
GKDKAGVRNC PPQSSAHLAP PRPSLTEQFK TVGNRVAVLA TVLAILNTRT FRLNVEGGPR
LVDLPWLWKS VYVVICGCGT YVVIDVSHRL WMLLLVLACV RQPSDFHPVF GSMADAYTLQ
RFWGRSWHQI HRRKFLAHAE FITRDLLGLP ERSTSAATIK LYTSFFISAL IHAGGDYACL
RGSSVVKTNY FGGGGSIPFF LLQALAIHVE SMLIAGFRRM ELQVAQTDDL SNIFQNLRSK
NTDLRDRAAE DLRRYVVTKV SEMTPDAAAK IWDDTINRNL FDLMHSQSNT DRFGGLLAID
HLLYPNGEET IESKRHLYRF YNYVRHQLPN HDINLMLAAS KTLGQIAHAG GAAFGDKFMD
YEVQGAIELM QPDKQESPRY AGVLILKELA KNSPSHFSSH IGVVLDNIIL PLRDPRVIVR
EGAAELLAAC LEIITKREKQ SRNAHLQKIL QDAQLGLRQS QPEVIHGSLL TYRELLIYGK
MFFKDAFVDA AETILRFKSH RDSLVRKMVI TLIPTLAAQM NALLASFIAI GHTAAAINGD
MKPFLEPIMS HVKLGLQARG KKNAPSEEPI FQCVGMLAKA VGPNLTKLLH DQLDLMFACG
LSGALISALK EITTNIPPLL KTIQDRLLDI LSLILSNQPY KPLGAPPSLG RDANVVAREL
STTQINEHNS DRITLALTTL GDFDFSGHVL NEFVRNCALP YLESDNAEIR EAAAVTCCRL
FVQDPICYQA SNHAIEIISD VLDKLLTVGI ADPDAKIRHV VLSNLHERFD KHLAQAENVR
SLFIALNDEE FKNRVTAVGL IGRLARHNPA YVMPALRKAF IQLLTELEYS GVMRNREECT
RLLTLLVSAT QRLIKPYALS MLRALLPKAN DSNPTVASNV MTCLGELVCV AGEDAMPNVP
DLMRVIIDRL NDPALVKRDA ALHTLGQVCS STGYVIQPLV DYPQLLPTLV RILRTENTVF
AKREVVKVLG ILGALDPFRR KSKTQEEPPP EPAEAPAGSA SAVAAAAAAA QANVAVGTDD
YFQTAVITSL LAVLKDPSLS GHHHTVIEAI MSIFKTQGLK CVTFLPQIIP AFSLVARTST
VRMQEFHLQQ LAILVAIIKQ HVRNHAMRLY RLIIELWDNP ALHLPLVSLI EALGNALDSE
FKPFLATLIP LILKIFDQEL TDKRMLTQIK IFDAFVTFGT NIEEYLQLVI PVIVRTYERT
DASSALRKKA IHTIESLSAR VNFSDHASRI IHPLVRVLDT AGNDIRQTAL DTLCAFVYQL
GSDFAIFVST IQKVMAKHRI THPKYEGLIA KLLNGEHLVQ EADSSKSQDL PAPAEATKLT
VNQQHLKQAW DTSQVSTLED WADWMHRLEV EFMKESPSHA LRACMSLVDS HPPLAKELFN
AAFLSCWGEL YDQYQEDLVR SIEFAITSST ASTDLIHRLL NLAEFMEHEE KPLPIEHRTL
GEYAIKCRAY AKALHYKELE FFSESSPTII ESLISINTWL QQHDAAWGTL LTAGEQYDVT
KHEEWYEKLG RWQEALHAYE KKAETSPSAP GIAIGRMKCL HALGEWDQLA ALVEDHWPNA
NPEDRREIAP MAAAAAWSLR EWDAMEGYIG TMRADVADKY FYRAILSVHQ NQFPKAMIHI
GKARDHLKND MSSFVGEGYG QSYNTMVRAQ TLSELEEIIA YKQFADQPER QETIRATWVK
RLQGCQPDVE VWQRILQVRT LVLGPEDDPV MWIKFANLCR KSERMVLAEK TINSLLTPEK
APPEVVYAQL KFMWATGAKE ASLEFVRRFA TNLAKDIEHE SGDSVPKSSV SKTRLDEFNK
LLARCYFKQG QWQKELKEDW NQRNIDDILR SFQSATRHDP TWYKAWHTWA LANFEVIGFM
ENLEPRSGST RSNKMAAHVV QAVEGFFRSI SLRNEDALQD TLRLLTLWFK YGAHDEVSHA
MASGFSTVEV DTWLEVIPQI IARIQTPHIN IRRNINALLI DVGKHHPQAL VYPLTVASKS
SSKSRQTAAA SIMERMREHS AEIVNQALLV SRELIRVAIL WHELWHEGLE EASRLYFTEN
NPEGMIMALE PLHEMIAAGP TTAREISFVQ VFGRELHEAR EACRRYHDYG DTAELDKAWD
IYYGVFKKVE KQLPQLTTLD LQYVSPALLK SRNLELAVPG TYQSGRPIIK IVSFATKLTV
ISSKQRPRRL SLVGSDGKNY HYVLKGHEDL RQDERVMQLF SLVNTLLSAD TDSFQRRLHI
QRYPVIPLAP NAGLLGWVQD SDTLHVLVRD YRESRKVLLN IEYRLMLQMA PDYENLILLQ
KVEVFEYALE NTTGQDLYRV LWLKSTTSEH WLERRATYTR SLAVNSMVGH ILGLGDRHPS
NLLLERATGK VVHIDFGDCF EVAMHREKFP EKVPFRLTRM LTHAMEVSGI EGSFRRTCEI
SMRVLRDNKE SLMAVLEAFV YDPLINWRLM QAEVDVRRQE DSETDPDRAA ELARLAAHPQ
GPSRKLKADE NDIFNETMGG LGAQEVRNER ALAVYNRVQH KLTGRDFNPD VALNVSAQVD
KLILQATSLE NLCQCFSGWC AFW
//
