ID M1CF01_SOLTU Unreviewed; 2447 AA.
AC M1CF01;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN Name=102604383 {ECO:0000313|EnsemblPlants:PGSC0003DMT400066097};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400066097, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400066097}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400066097};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 EnsemblPlants; PGSC0003DMT400066097; PGSC0003DMT400066097; PGSC0003DMG401025733.
DR Gramene; PGSC0003DMT400066097; PGSC0003DMT400066097; PGSC0003DMG401025733.
DR HOGENOM; CLU_000178_7_1_1; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1CF01; baseline and differential.
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; 5.
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; 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 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:UP000011115};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU364109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT DOMAIN 1298..1855
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2033..2350
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2415..2447
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2447 AA; 275454 MW; FDE4FE1F48B11529 CRC64;
MATTVQAIRY PVATTGAGNI DALNRVLADL CSRGNPKDGA ALTLRRLVEE EARDLSGEAF
ARFMDHLYER ITTFLDSNEV SENLGALRAI DELIDVTISE NASKVAKFSN YMRVAFETKR
DPEILVLASK VLGHLARSGG AMTADEVERQ VKVALEWLRG ERIEYRRFAA VLILKEMAEN
ASTVFNVHVP EFVDAIWVAL RDPTLAVREK AVEALRACLR VIEKRETRWR VQWYYRMFEA
TQDGLGRNAP VHSIHGSLLA VGELLRNTGE FMMSRYREVA EIVLRYLEHR DRLVRLSITS
LLPRIAHFLR DRFVTNYLTI CMNHILHVLK IPAERASGFI ALGEMAGALD GELINYLPTI
TSHLRDAIAP RRGRPSLEAL ACVGNIAKAM GPTMEPHVRG LLDPMFSAGL SVTLVDSLEL
LTESIPPLLP TIQNRLLECI SAILSRSHHA MSRQSAALSR GHLATVTPQV PELSGSALVQ
LALQTLARFN FKGHDLLEFA RESVVVYLED EDGATRKDAA LCCCKLIANS FLAMSSTQFS
PSRINRASGK RRRLVEEIVQ KLLIAAVADA DVTVRHSIFS SLYADGGFDE FLAQADSLTA
IFATLNDEDF EVREYAISLA GRLSEKNPAY VLPALRRHLI QLLTYLEQSA DNKCKEESAK
LLGCLIRNCE RLVLPYVTPI HKALVAKLCE GTGVNANSGI ISGVLVTVGD LARVGGFAMR
QYISELMPLI VEALLDGAAV TKREVAVSTL GQVVQSTGYV ITPYNEYPQL LGLLLKLLNG
ELAWSTRREV LKVLGIMGAL DPHVHKRNQQ SLPGSHGEVT RVTGDPGQHI RSMDELSTDL
WPSFATSEDY YSTVAINSLM RILRDPSLSS YHQKVVGSLM FIFKSMGLGC VPYLPKVLPD
LFHIVRICED GLKEFITWKL GTLVSIARQH IRKYLPELLS LISELWSSFS LPVANRPVHI
APILHLVEQL CLALNDEFRK YLPDILPCCI QVLTDAERFN DYTYVIPILH TLEVFGGTLD
EHMHLLFPAL IRLFKVDASV EVRRGAIKTL TRLIPCVQVT GHISSLVHHL KLVLDGNKEE
LRKDAIDALC CLAHALGEDF TIFIPSIHKL MVKHRLQHKE FEEIQGRLEK REPLIFGSTT
AQRLNRRLPV EVISDPLSDG ESDLYEVGTD MQKQLRNHQV NDGRLRTAGE ASQRSTKEDW
AEWMRHFSIE LLKESPSPAL RTCARLAQLQ PFVGRELFAA GFVSCWSQLN EASQRQLVRS
LEMAFSSPNI PPEILATLLN LAEFMEHDER PLPIDIRLLG ALAEKCRAFA KALHYKEMEF
EGALSNRRDA NPVAVVEALI HINNQLHQYE AAVGILTYAQ QHLGVQLKES WYEKLQRWDD
ALKAYTAKAS QASSSHLCLD ATLGRMRCLA ALARWEELNN LCKEYWTPAE PAARLEMAPM
AANAAWNMGE WDQMAEYVSR LDDGDETKFR VLGNTASSGD GSSNGTFFRA VLLVRRGKVL
ESYERAYSNM VRVQQLSELE EVIEYCTLPP MGNPVAEGRR ALVRNMWNER IKGAKRNVEV
WQVLLAVRAL VLPPTEDIET WIKFASLCRK NGRISQARST LIKLLQFDPE TTPATGRYHG
PPQVMLAYLK YQWSLGEDHK RKEAFARLQD LAMDLSRTAT LQPVMQNALV ASSGAPLVAR
IYLRLGTWKW ALSPGLDDDS IQEILSAFRN ATHCATKWGK AWHTWALFNT AVMSHYTLRG
FANIAAQFVV AAVTGYFHSI ACGAHAKGVD DSLQDILRLL TLWFNHGATS EVQMALQKGF
THVNINTWLV VLPQIIARIH SNNHAVRELI QSLLVRIGQS HPQALMYPLL VACKSISNLR
RAAAQEVVDK VRQHSGVLVD QAQLVSKELI RVAILWHEMW HEALEEASRL YFGEHNIEGM
LKVLEPLHEM LEEGAMRNNT TIKEKAFIQA YRIELLEAYE CCMKYRRTGK DAELTQAWDL
YYHVFRRIDK QLQTLTTLDL QSVSPELLEC RDLELAVPGT YRADSPVVTI ASFAPQLVVI
TSKQRPRKLT IHGSDGKDYA FLLKGHEDLR QDERVMQLFG LVNTLLENSR KTAEKDLSIQ
RYDVIPLSPN SGLIEWVPNC DTLHQLIREY RDARKITLNQ EHKLMLSFAP DYDNLPLIAK
VEVFEYALQN TEGNDLSRVL WLKSRTSEVW LDRRTNYTRS LAVMSMVGYL LGLGDRHPSN
LMLHRYSGKI LHIDFGDCFE ASMNREKFPE KVPFRLTRML VKAMEVSGIE GNFRSTCENV
MQVLRLHKDS VMAMMEAFVH DPLINWRLFN FNEVPQMSTL ASAHVPPVVN SEESSSDREL
LQPQRGARER ELLQAVNQLG DANEVLNERA VAVMARMSNK LTGRDFAATS ASSSSLQHPL
DHSTLISGET READHGLSVK LQVQKLIQQA MSHENLCQNY VGWCPFW
//
