ID A0A0B0NM31_GOSAR Unreviewed; 2448 AA.
AC A0A0B0NM31;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=F383_00374 {ECO:0000313|EMBL:KHG12829.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG12829.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-2014) 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; KN398398; KHG12829.1; -; Genomic_DNA.
DR Proteomes; UP000032142; 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: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: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 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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364109};
KW Reference proteome {ECO:0000313|Proteomes:UP000032142};
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 1288..1868
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2031..2349
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2416..2448
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 808..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2448 AA; 275203 MW; 5209D15DBBE524D4 CRC64;
MAVTLQSLRF CGLAASGPAG GSFEALNRIL ADLCTRGNPK EGTSLALKKH VEEEARDLSG
EAFSRFMDQL YDRISSLLES NDVAQNMGAL RAIDELIDVA LGENASKVSR FSNYMRTVFE
TKRDPEILVL SSKVLGHLAR AGGAMTADEV EFQVKTALQW LRGDRIEYRR FAAVLILKEM
AENASTVFNV HVPEFVDAIW VALRDPTLAV RERAVEALRA CLRVIEKRET RWRVQWYYRM
FEATQDGLGK NAPIHSIHGS LLAVGELLRN TGEFMMSRYR EVAEIVLRYL EHRDRLVRLS
ITSLLPRIAH FLRDRFVTNY LTICMNHILT VLRIPAERAS GFIALGEMAG ALDGELVHYL
PTITSHLRDA IAPRRGRPSL EALACVGNIA KAMGPAMESH VRGLLDIMFS AGLSPTLVEA
LEQITVSIPS LLPTIQDRLL DCISLVLSKS HYFQARPAVA RGTATNIPQP VAELSGSAHV
QLALQTLARF NFKGHELLEF ARGSVVRYLD DEDGATRKDA ALCCCKLVAN SFSDITSSQF
GSGRSSRAGG KRRRLIEELV EKLLIAAVAD ADVTVRHSIF SSLHGNRGFD DFLAQADSLS
AVFAALNDED FDVREYAISV AGRLSEKNPA YVLPALRRHL IQLLTYLGQS ADNKCREESA
KLLGCLIRNC ERLILPYIAP VHKALVARLL EGTGVNANNG FISGVLVTVG DLARVGGFAM
REYISELMPL IVEALLDGAA VTKREVAVAT LGQVVQSTGY VIAPYNEYPQ LLGLLLKLLN
GELVWSTRRE VLKVLGIMGA LDPHAHKRNQ QSLSGSHGDV THAASDSGQH IPSSMDELPM
DLWPSFATSE DYYSTVAINS LMRILRDPSL ASYHQKVVGS LMFIFKVLHD LFQIVRTCDD
HLKDFITWKL GTLVSIVRQH IRKYLPELLS LISELWSLFS LPASTRPSRG FPVLHLVEQL
CLALNDEFRK YLPAILPCCI QVLSDAERCN DYTYVLDILH TLEVFGGTLD EHMHLLLPAL
IRLFKVDGSV EIRRAAIRTL TRLIPCVQVT GHISSLVHHL KIVLDGKNDE LRKDAVDALC
CLAHALGEDF TIFIPSIHKL LLRHRLQHKE FEEIEGRLRR REPLIVGSTA AQRLSRRPPV
EVVSDPLNDM ENDPYEEGND VQKHPRGHQV NDGRLRTAGE ASQRSTKEDW AEWMRHFSIE
LLKESPSPAL RTCARLAQLQ PFVGRELFAA GFVSCWSQLN ESSQRQLVRS LEMAFSSPNI
PPEILATLLN LAEFMERDER PLPIDIRLLA ALAEKCRAFA KALHYKEMEF EGARSKKMDA
NPVAVVEALI HINNQLHQHE AAVGILTNAQ QYLDVQLKES WYEKLQRWDD ALKAYTAKAT
QASSPHLVLE ATLGRMRCLA ALARWEELNN LCKEYWTPAE PSARLEMAPM AANAAWNMGE
WDQMAEYVSR LDDGDETKLR ALGNTAATGD GSSNGTFFRA VLLVRRGKYD EAREYVERAR
KCLATELAAL VLESYERAYS NMVRVQQLSE LEEVIDYCTL PMGNPVAEGR RALIRNMWTE
RIQGAKRNVE VWQVLLAVRA LVLPPTEDIE TWLKFASLCR QNGRISQARS TLIKLLQYDP
ETAPENVRYH GPPQVMLAYL KYQWSLGDDL KRKEAFSRLQ NLARELSISP NIQSIPSTAS
MNGTSANVPL LARVYLKLGA WQWTLSSPGL DDDSIQEILS AFRNATQFAP KWAKAWHAWA
LFNTAVMSHY ARGLQTIASQ FVVSAVNGYF HSIACAANAK GVDDSLQDIL RLLTLWFNHG
ATAEVQMALQ VGFAHVNINT WLAVLPQIIA RIHSNNHAVR ELIQSLLVRI GQSHPQALMY
PLLVACKSIS NLRKAAAQEV VDKVRQHSGV LVDQAQLVSK ELIRVAILWH ELWHEGLEEA
SRLYFGEHNI EGMLKVLEPL HEMLEEGAMR DNTTIKERAF IEAYHHDLSQ AYECCMKYKR
TGKDAELTQA WDLYYHVFRR IDKQLQKCRD LELAVPGTYR AESPVVTIAS FAHQLDVITS
KQRPRKLTIH GSDGEDYAFL LKGHEDLRQD ERVMQLFGLV NTLLENSRKT AEKDLSIQRY
EVIPLSPNSG LIGWVPNCDT LHQLIREYRD ARRITLNQEH KFMLSFAPDY DHLPLISKVE
VFEYALQNTE GNDLAKVLWL KSRTSEVWLE RRTNYTRSLA VMSMVGYLLG LGDRHPSNLM
LRRSSGKILH IDFGDCFEAS MNREKFPEKV PFRLTRMLVK AMEVGGIEGN FRLTCENVMQ
VLRSNKDSVM AMMEAFVHDP LINWRLFNFN EVPQMSIFAS THGTAVTNTE ETAPSKELAQ
PQRGAREREL LQAVNQLGDA NEVLNERAVV VMARMSNKLT GRDFLSCSSI PTASSNIQHS
IDHSTLISGD NREVEHGLSV KLQVQKLIIQ ATSHENLCQN YVGWCPFW
//
