ID A7RU99_NEMVE Unreviewed; 2475 AA.
AC A7RU99;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=NEMVEDRAFT_v1g162805 {ECO:0000313|EMBL:EDO44977.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO44977.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO44977.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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; DS469539; EDO44977.1; -; Genomic_DNA.
DR RefSeq; XP_001637040.1; XM_001636990.1.
DR STRING; 45351.A7RU99; -.
DR EnsemblMetazoa; EDO44977; EDO44977; NEMVEDRAFT_v1g162805.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000178_7_1_1; -.
DR InParanoid; A7RU99; -.
DR OMA; MRQHSAK; -.
DR PhylomeDB; A7RU99; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
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; 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 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:UP000001593};
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 1352..1911
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2085..2397
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2443..2475
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 526..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2475 AA; 280273 MW; 257C68DD562D232D CRC64;
MQQLRPQLLS GLKSRSDESR LQAAKDLQHY VSTELREASP EQYGSFMDEF NHHIFEMVSS
SDANEKKGGI MAIVGLIGIS GGSATKVSRF ANYLRNLLPS NDTAVMEMAS KAMGRLALTG
GTFTADYVEF EVKRALEWLG GDRNEGRRHA AVLVLRELAV NAPTFFFQQV QPFFDNIFNA
VRDPKQAIRE GAMEALRACL VILAQRETKE IRKPPIWYSQ TYEEAKKGFE GSTNTKEKGV
VLTKEDKAHG SLLIINELIR SASLEGEQYK KDLEDIYCDQ VQSNVMSLND LGITSPKSKF
SYQTGSHTHP TLSSLASGTQ LGEINPLCHS KVCKEFMEDK FDEVCILVLY YSGTRNSTIQ
QTLLTLLPRL AAFQPQKFVK KYLKESMQYL VGALKRDRER SSAFKAIGLL AIAVRHNIEP
FSKPVVEQVK QSLPMRDLGH KRQKAVTVDP MVFACVAMLS RAIGPKISKD VKELLEPMLS
VGLSPALTAC LHDLAHQVPQ LKKSIQDGLL KMLSLILMQK PLRHPGAPKS TPALTPSTSS
HSLFDSSDVT STVLALRTLG SFDFEGHLLT HVNLVRNCAE TFLASEFKDI RMEAVRTCSR
LLSPSLHPMV VTNAPQHGPI SATSTQVVSE VLSKMLMVGI TDPDPDIRHC VLSSLDERFD
AHLAQAENLA ALFVALNDEE FEIREVAISI ISRLSNLNPA YIMPSLRKAL IQILTELEYS
GVGRSKEQSA RMLGHLVSNA PMLIRPYMEP ILKALIPKLR DPDPEVVISV LAAIGEHAQV
SGTKMCKWMN ELFPIIIDML QDASSMAKRK IALWTLGQLV ESTGYVVEPY RKYPNLLEVL
LNFLKTEQAP GIRREAIRVL GLLGALDPYK HKLNQIEGVL DDGGISTGSK ESETAVCDDR
VDTSTSEMLV TMGSVVLEEF YPAVVISALM RIVRDPSLSS HHTMVIQAVT FIFKSLGMKC
VTYLSQIMPS FLNVIRTCDS GFREFVFQQL GVLISIVKQH IRNYLDDIFT LIKEYWTINS
PMQTTIVLLV EQIAVALGGE FKNYLPQIIP HILKVFMHDN SPQRSVTTKL LNALQMFGSS
LDDYLHLLVP PVVKLFDSNE IPLSVRKCAL ETLDRLSESL DLTDFASRII HPIVRTLDSC
SELRGTAMDT LSSLVFQLGK RYSTFIPTVN KVLIKHKIQH QRYDVLICKI VKSNFVLDWE
NDLLLRRQKL VRGNFADDSA TTAAIEAASI KKLAFKPDSL QKAWGASRCV SKDDWMEWLR
RLSVELLKES PSPALRSSWA TAQTYPPLAR DLFNAAFVSC WSELHEELQN ELVKNLELAL
KSQIPEITQT LLNLAEFLEH TEKGALPLSS DLLGEQASKC RAYAKALHYK EEEFHRVPNT
ETLEALISIN NKLQQPEAAH GVLVYAQRMH GADEIRERWY EKLHDWENAL NAYKKKLDQD
PEDIHLTLGR MRCMEALGEW GELHTVACDK WPDVSDDIRK QMARMAAAAA WGLGNWESME
EYTCLIPRDT QEGAFYRAAL ALHHDNFQQA QACIDAARDL LDTELTARAG ESYNRAYGAM
VSVQMLSELE EIIQYKLVHE RREDIKRTWW NRLQGCQRVV EDWQKILQVR SLVLTPQEDM
QSWLKYSSLC RKSGRLALSH KTLVMLLGSD PSKHPDLPLP TTYPQVTFAY MKHLWREGQK
EEAFQHLHFF VHTTLHQQAL QSLSPNDDDN KREELLKLVA RCYLKLGDWQ SSLQGFNENT
IPQILLYYSA ATENDKSCYK AWHSWAFMNF EAVLYYKNQQ EKEKSEGLSP GHPSSPSASP
KTVNPVITYA KPAVHGFFKS IALSSGNSLQ DTLRLLTLWF DYGHLPEVYE ALVEGIKTIQ
IDTWLQVIPQ LIARIDTPRQ LVGRLIHQLL TDIGKHHPQA LIYPLTVASK SASSARHNAA
NQILKNMCEH SQQLVQQAVM VSEELIRVAI LWHELWHEGL EEASRMYFGE GNVKGMFAVL
DPLHQMMERG PQTLKETSFN QAYGRDLMEA QEWCRRYQKS GNVKDLTQAW DLYYTVFRRI
SKQLPQLTSL ELQYVSPKLL MSRDLELAVP GTYEPHKPVI HIRNVHSSLN VITSKQRPRK
LCLAGSNGSD FMFLLKGHED LRQDERVMQL FGLVNTLLAS DPETSKRHLS IQRYAVIPLS
TNSGLIGWVP HCDTLHALIR DYREKKKILL NIEHRIMLTM APDYDHLTLM QKVEVFEHAL
ANTNGDDLAK LLWLKSPSSE VWFDRRTNYT RSLAVMSMVG YVLGLGDRHP SNLMLDRLTG
RILHIDFGDC FEVAMTREKF PEKIPFRLTR MLTNAMEVTG IDGNYRLTCE SVMRTMREHK
DSVMAVLEAF VYDPLLNWRL MDNAAPKIKR SKGRSDTMTE AAEEMLEGVD VNRDKPSAKK
PAEPLHSIEE ETGHKPEFLN KKALDIITRV RDKLTGRDFA NRNTLDVPTQ VDLLIKQATA
HENLCQCYIG WCPFW
//
