ID A0A1X6N669_9APHY Unreviewed; 2345 AA.
AC A0A1X6N669;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=POSPLADRAFT_1065405 {ECO:0000313|EMBL:OSX64010.1};
OS Postia placenta MAD-698-R-SB12.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX64010.1, ECO:0000313|Proteomes:UP000194127};
RN [1] {ECO:0000313|EMBL:OSX64010.1, ECO:0000313|Proteomes:UP000194127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX64010.1,
RC ECO:0000313|Proteomes:UP000194127};
RG DOE Joint Genome Institute;
RA Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL Submitted (APR-2017) 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; KZ110594; OSX64010.1; -; Genomic_DNA.
DR STRING; 670580.A0A1X6N669; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000194127; 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: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; 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: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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364109};
KW Reference proteome {ECO:0000313|Proteomes:UP000194127};
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}.
FT DOMAIN 1248..1795
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1969..2283
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2313..2345
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2345 AA; 265913 MW; 916C7CDF56707961 CRC64;
MASTSSAPQG DPLDNIFQGL RSKSHETRVQ SAIELQRYVS NTVHDGFTDT AAKLWDDRIN
RRIFELIHSQ NTADNLGGVL AIDYLLNAEG EGAIEYRENL YRFYNYVRTL LPSSDIDVML
AASKTLGHIA AVGGGSSLLG NSWLDKEVPI AITLLQADKQ EPGRYAGVLI LKELARNSPT
FFHSHIGLVF EKILTPLRDT RIIVRESAAE LLAACLEIIT QRERQTPSPY LMKILSDAQL
GLRMAQPEVI HGSLLTYREL LLHGGMFMKE NFLDAAEQIL TFKIHKDALV RKMVITLIPT
LAVYDPQTFS EHYLHRAMGH LVTQLDKPNE RSVAFIAIGH VASAMGSDMK PFLDSVMAHI
KQGLQIRGYA KKNAPSEAPI FQCVGMLASA VGPNLTKLLH DQLDLMFACG LSEPLRQALT
AIAAHIPPLL KTIQDRLLDL LSLILSGQHY KPLGAPASLL RADSSKDGGA AEGQGGQKNS
ELITLALITL RDFDFSGHVL NAFIRDCALP YLEEDNAGVR RVAAETCCRL FMRDPIVYQA
SNHSIEIISD VIDKVLTVGI ADPDPTIRQI VLSSLHERFD KHLAQAENVR ALFIAVNDEV
FENRVTAVSL IGRLALHNPA YVMPSLRKIL IQLLTELEYS TVTRSREECT RLLTLLVSAT
QRLIKPYAIP MLRVLLPKAN DPNPTVAANI LMCLGELTRV GGEDVTPNVP ELMQVILSKL
ADPSLPKRDA ALHTLGQVCS STGYVVTPLV DYPQLLQILN RILKTETKLS VKREVVKVLG
ILGALDPYRR RAKPEEEVTT EMSSHLVAAI SRNYSGANTA SDDYYQAVAI NALLDILKDQ
QASERHHTVI EAIMSIFKTQ GLKCATFLPQ IIPAFASVAR ASAARIQVFH LEQLAILVGI
IKQHVRNYMP HIFSLITDLW ENAPLRLPLV SLIEALGKAL DAEFKPFLPT ILPLVLKVFD
GEFNEKATST QIKIFDAFLT FGANIEEYLQ LVIPIIVKTF EKTEAPIPLR KKAIQTIDGL
SRKVNFSDHA SRIIHPLVRV LNDSTNDMRM TVMDTLCTMV LQLGSDFAVF VPTVNKCLVR
NRVSHPRYEN LVSKLLNGER LPQEAGLAEF PESSKAAELS APAEATRMTV NQQHLRDAWD
VSQVSGKDDW IKWMHGISVE FMKESPSHAL RACMSLVDIH QPLAKELFNA AFISCWGELF
DHFQEDLVRS IECAITSPHA PSEVVHRLLN LAEFMEHEEK PLPIENRVLG EYAMKFHAYA
KALHYKELEF FTETSPTIIE SLLGINSKLQ QHDAAWGTLL IAREQYDVSK HEEWYERLGR
WQEALKTYGK KLEDDPDNLD VAIGRMRCLH ALGEWNDLAA QVDEHWSKAS HEDRREIAPM
AAAAAWSLND WESMEDYIAT MKLDSADRPF YRAILSVHQN QFAKAMAHIA KARDMLEPEL
TSLVGESYGR SYNIMVRAQM LSELEEIIAY KQYADQPDRQ LAMRSTWMKR LQGCQPDVEV
WQRILQVRAL VVTPEDDPVM WIKFANLCRK NDRMFLAEKT INSLLTPDRH TKATSIVVYA
HLKYTWAAGN RQESLTHLRQ LASNLQRTLQ AETSVHQSDL ARPKANQKLE EISRLLARCY
FKQGQWQVAL HEDWGHRNVK DILHSYFLAT HYDSTWYKAW HTWALANFEV VGYLETQVEN
KMTGVPPDDL AVHIVQAVDG FFRSISLRNE NALQDTLRLL TLWFKYGAHE DVSHAMSSGF
TDLEVDTWLE VIPQIIARIQ TPSANIRRNL NNLLIDVGKH HPQALVYPLT VASKSSSEVR
KKAALNIMNR MREHSPTIVD QALLVSHELI RVAILWHEMW HEGLEEASRL YFTDHDPEGM
IVFLEPLHEM LEAGPKTARE TSFTQVFGRD LHEAREACRH WRTYGEQRDL DRAWEIYYSV
FKKVESQLRQ LTTLDLQFVS PELLKARDLE LAVPGTYQSG RPIVTIIYFA TKLSVIQSKQ
RPRRLSLKGS DGRDYQFVLK GHEDLRQDER VMQLFSLVNN LLSVDTDCFK RRLHIQRFPV
IPLAPNAGLL GWVQDSDTLH VLVRDYRESR KILLNIEYRL MLQMAPDYEN LILLQKIEVF
EYALENTTGQ DLYRVLWLKS ANSEHWLERR ATYTRSLAVN SMVGHILGLG DRHPSNLMLE
RNTGKMVHID FGDCFEVAMH REKFPEKIPF RLTRMLTHAM EVSGIEGSFR NTCEISMKVL
RDNKESLMAV LEAFVYDPLI SWRLMQTDAE SRQVKDRPEA SRTTAFPQGP IRKLKADEND
IFNEHHEVRN ERALSVYNRV QHKLTGRDFN PDVSLTVAAQ VDKLIIQATS LENLCQCFSG
WCAFW
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