ID A0A0C9ZTS1_9AGAM Unreviewed; 2364 AA.
AC A0A0C9ZTS1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=PISMIDRAFT_679672 {ECO:0000313|EMBL:KIK23043.1};
OS Pisolithus microcarpus 441.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK23043.1, ECO:0000313|Proteomes:UP000054018};
RN [1] {ECO:0000313|EMBL:KIK23043.1, ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|EMBL:KIK23043.1,
RC ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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; KN833731; KIK23043.1; -; Genomic_DNA.
DR STRING; 765257.A0A0C9ZTS1; -.
DR HOGENOM; CLU_000178_7_1_1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000054018; 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:UP000054018};
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 1247..1800
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1974..2287
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2332..2364
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 789..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2364 AA; 268098 MW; A8F154F95069B145 CRC64;
MASTISPMHT DNLSQIFQGL RSPTPDTRLQ AAIDLRRYVV TTVVEMPSDA AVKLWDDDIN
KRLFDLMHSQ NNTERLGGLL AIDHLLENDG EDLVGSKRYL YRFYNYVKQL LPNHDMNIML
AASKTLGHIA AIGGADFGEG FMDAEVPAAV DMLQGQELPR YAGVLILKEL ARNSSAYFHS
HISLVFDKIL IPLRDPRVFV REGAAELLAA CLDIVTNRER QTRPMYLMKI LQDAQLGLKM
SQPEVIHGSL LMYRELLLRG DTFMREAFLD TAEQILRFKS HRDNLVHKTV ITLIPTLAAY
ETHTFTEHYL HKSMGHLLTQ LEKPNERYFA FIAIGHIAAA VGSDMKPFLD SIMLQIKRGL
QQRGKKNAPS EEPIFQCVGM LASAVGPNLT KLLHDQLDLF FACGLSEPLR QALTDIARNI
PPLLKTIQER LLDLLSSILC GQPYKVIGAP PSLVRGDVAS YAREFSASQA AKTGRNSELI
TLALSTLGSF DFSGHVLNEF VRGAALPYLD DDNPDVRRAA ALACCRVFVK DPICYQASSH
AIEIISDVLD KLLTVGIADP EPSIRLTVLS SLHERFDKHL AQAENVRSIF IALNDEIFEN
RVTAVGLIGR LAKHNPAYVM PSLRKSLIQL LTELEYSTVT RNREECTRLL TLLASATQRL
IKPYALPILR VLLGKASDTN PTVAANVLMC LGELTAVAGE AVTPHIPELM QVIIAKLQDP
AHVKRDAALR TLGQLCSSTG YVIAPLVEYP QLLPILHRIL RTESGTSRRE VVREVVKVLG
ILGALDPYRR KTRPDDDPTA EGTLPANSTA VSSATSLTSS DDYFQTVVIT ALLAVLRDQS
MSSHHHSVIE AIMNIFKTQG LRCVTFLPQI IPAFAAVART SAARLQEFHL QQLAILVGII
KQHVRNYMPE VFGLVTELWE NVSLQLPIVS LVEALGKALD AEFKPFLPTI LPHLLKVFEG
ELTDKRMNTQ IKIFDAFLTF GSNIEEYLHL VIPVIVKTAE RVEASTILRK RAIQSIAHLS
QRVNFSDHAS RIIHPLVRVL DVPNNELRQA VMDTLCAIVV QLGSDFAVFV PMINKCLHRN
RIHHPRYENL IGKLLNGERL PQESGIHELL ESSKVAEISV VAEPAKLTVN QQHLKQAWDV
SLVAEKEDWV EWMHRLSVEF MKESPSHALR ACMSLVDIHP PLAKELFNAA FISCWTELYD
QYQEGLVRSI EQAITSPKAP SELIHRLLSL AEFMEHEEKP LPIEHRTLGE YAMRFHAYAK
ALHYKELEFF TETSPNIIEA LIGINTKLQQ HDAAWGTLTI AREQFDVSKH EEWYERLGKW
QEALVAYEKK ATIDPDSPEV QIGRMKCLHA LGEWEQLEQQ VLETWTSASC EERREIAPMA
AAAAWSLHDW EAMDDYIGGM RVDSPDRAFY RAILSVHQNQ FPKALKEIGK ARDLLEPELT
SFVGEGYGRS YNTLVRAQML SELEEIIMFK QYADQPERQQ AMRKTWMKRL QGCQPDVETW
QRILQVRALV LNPEDDPVMW IKFANLCRKS DRMALAEKTI NSLLSPERLQ HLRDDQHMKA
PPNVVYAQLK YMWASGAQED SLSFLRQFSA NLARDLQTEN KEHFQRTSVG KQKLEELSRL
LARCYFKQGQ WQVELKEDWG ARNVKDILHS YLLATHYDPN WYKAWHTWAL ANFEVVGYLE
SQKESAVSDV PGSGLAAHTV QAVRGFFRSI ALRNENALQD TLRLLTLWFK YGAHDDVSQA
MAEGFSAVEV DTWLEVIPQI IARIQTPIAN VRRNINNLLT EVGKHHPQAL IYPLTVASKS
SSATRQNAAL LIMDRMKEHS PIIVEQALLV SQELIRVAIL WHEMWHEGLE EASRLYFNDK
NPEGMITTLE PLHELLERGP TTAREISFIQ AFGRDLREAR EACRRYRECG EMTELNKAWD
IYYGVFRKVE KQLPQLTTLD LQYVSPQLLK ARNLELAMPG TYQSGRPVTK IAGFATKLTV
IASKQRPRRL SLKGDDGKDY MYVLKGHEDL RQDERVMQLF SLVNTLLSVD TNSFKRRLHI
QRYAVIPLAP NAGLMGWVKD SDTLHVLVRD YRDSRKVLLN IEYRLMLQMA PDYENLTLLQ
KVEVFEYALE NTTGQDLYRV LWLKSANSEH WLERRATYTR SLAVNSMVGH ILGLGDRHPS
NLLLERTTGK VVHIDFGDCF EVAMHREKFP EKIPFRLTRM LTHAMEISGI EGSFRHTCEI
TMSVLRANKE SLMAVLEAFV YDPLINWRLM QADVDARRQD DTDVDPGRAA ELAKVAAYPQ
APTRKLRADE NDIFNEAVDG PFARQEVRNE RALAVYNRVQ HKLTGRDFDP NVVLPVKVQV
DKLILQATSL ENLCQCFSGW CAFW
//
