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Database: UniProt
Entry: A0A6A4QFC0_LUPAL
LinkDB: A0A6A4QFC0_LUPAL
Original site: A0A6A4QFC0_LUPAL 
ID   A0A6A4QFC0_LUPAL        Unreviewed;      2471 AA.
AC   A0A6A4QFC0;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   08-OCT-2025, entry version 22.
DE   RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|ARBA:ARBA00069838, ECO:0000256|RuleBase:RU364109};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513, ECO:0000256|RuleBase:RU364109};
GN   ORFNames=Lalb_Chr05g0210831 {ECO:0000313|EMBL:KAE9612798.1};
OS   Lupinus albus (White lupine) (Lupinus termis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3870 {ECO:0000313|EMBL:KAE9612798.1, ECO:0000313|Proteomes:UP000447434};
RN   [1] {ECO:0000313|Proteomes:UP000447434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Amiga {ECO:0000313|Proteomes:UP000447434};
RX   DOI=10.1038/s41467-019-14197-9;
RA   Hufnagel B., Marques A., Soriano A., Marques L., Divol F., Doumas P.,
RA   Sallet E., Mancinotti D., Carrere S., Marande W., Arribat S., Keller J.,
RA   Huneau C., Blein T., Aime D., Laguerre M., Taylor J., Schubert V.,
RA   Nelson M., Geu-Flores F., Crespi M., Gallardo-Guerrero K., Delaux P.-M.,
RA   Salse J., Berges H., Guyot R., Gouzy J., Peret B.;
RT   "Genome sequence of the cluster root forming white lupin.";
RL   Nat. Commun. 11:492-492(2020).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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:ARBA00048679};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00047899,
CC         ECO:0000256|RuleBase:RU364109};
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC       {ECO:0000256|ARBA:ARBA00011031, ECO:0000256|RuleBase:RU364109}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAE9612798.1}.
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DR   EMBL; WOCE01000005; KAE9612798.1; -; Genomic_DNA.
DR   OrthoDB; 381190at2759; -.
DR   Proteomes; UP000447434; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0031931; C:TORC1 complex; IEA:TreeGrafter.
DR   GO; GO:0031932; C:TORC2 complex; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0016242; P:negative regulation of macroautophagy; IEA:TreeGrafter.
DR   GO; GO:0031929; P:TOR signaling; IEA:TreeGrafter.
DR   CDD; cd05169; PIKKc_TOR; 1.
DR   FunFam; 1.10.1070.11:FF:000017; Serine/threonine-protein kinase TOR; 1.
DR   FunFam; 1.20.120.150:FF:000001; Serine/threonine-protein kinase TOR; 1.
DR   FunFam; 1.25.10.10:FF:000265; Serine/threonine-protein kinase TOR; 1.
DR   FunFam; 1.25.10.10:FF:000284; Serine/threonine-protein kinase TOR; 1.
DR   FunFam; 1.25.10.10:FF:000288; Serine/threonine-protein kinase TOR; 1.
DR   FunFam; 1.25.10.10:FF:000474; Serine/threonine-protein kinase TOR; 1.
DR   FunFam; 1.25.10.10:FF:000802; Serine/threonine-protein kinase TOR; 1.
DR   FunFam; 3.30.1010.10:FF:000006; Serine/threonine-protein kinase 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; IPR050517; DDR_Repair_Kinase.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR009076; FRB_dom.
DR   InterPro; IPR036738; FRB_sf.
DR   InterPro; IPR057564; HEAT_ATR.
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; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF08771; FRB_dom; 1.
DR   Pfam; PF23593; HEAT_ATR; 1.
DR   Pfam; PF11865; mTOR_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   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Growth regulation {ECO:0000256|ARBA:ARBA00022604};
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:UP000447434};
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          1298..1878
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2056..2373
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2439..2471
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   2471 AA;  279053 MW;  A47449FD5913BF67 CRC64;
     MATSSQSHTH RYTAPPSVSG NFDTLNRILS DLCTRANPNE GSSLAFKKHL QQEQARDLTG
     EVFSRFMEHL YDRISNLLDS TDVADNLGAL RAIDNLIDDS LGENASKVSR FTTYMRTVFD
     SKRDPDILVH ASKVLGHFAR AGGAMTADEV ERQVQIALAW LRGTRLEYRR FAAVLILKEM
     AENASTVFNV HVPEFVDAIW VALRDPALPV RERAVEALRA CLRVIEPRET RWRVQWYYRM
     FEATQDGLGK NAPVHSIHGS LLAVGELLRN TGEFMMSRYR EVAEIVLRYL EHRDRLVRLS
     ITSLLPRIAH FLRDRFVTNY LTICMNHILS VLKVPQDRDS GFIALGEMAG ALDGELIHYL
     PTITTHLREA IVPRRSKPSL EALACVGSIA KAMGPATEPH VRGLLDIMFS TGLSTVLVEA
     LEQICTSIPS LLSTIQDRLL DSISMVLSKS HYHLGRSVAS MSRGTTMNVP QHFSELSGSA
     LVQLALQTLA RFNFKGHDLL EFVRESVVVY LDDEGRATRK DAALCCCKLV ANSFSGIMSI
     HFGSSHLNRS GGGKRRRLVE ELVEKLLISA VADADVTVRH SIFTSLHGDR GFDEYLAQAD
     NLSAVFAALN DEDFVVREYA ISLSGRLSEK NPAYVLPALR RHLIQLLTYL EQSADSKCKE
     ESAKLLGCLI RNCERLILPY IAPVHKALVA RLNDVNASTG IVTGVLVTVG DLARVGGFAM
     RQYIPELMPL IVEALLDGAS ISKREVAVAT LGQVVQSTGY VITPYNEYPQ LLVLLLKLLN
     GILVWSTRRE VLKVLGIMGA LDPHMHKRNQ KSLPGPHGEV TRPSSDSNQQ IQTMDEFPAD
     LWPSFASSDD YYSTVAINSL MRILRDPSLG IYHLKVIGSL MFIFKSMGLG CVPYLPKVLP
     DLFHTVRTCD DSLKDFITWK LGTLVSIVRQ HIRKYLQDLL SLISEFWSLF TLPPSSRPRF
     GYPVLHLVEQ LCLALNDEFR TYLPVILPGC IQVICDAERC NDYTYVLDIL HTLEVFGGTL
     DEHMHLLLPA LIRLFKVDAS VDIRRAAIKT LTRLIPRVQV TGHISSLVHH LKLVLDGKND
     ELRKDAIDAL CCLAHALGED FTIFIPSIHK LLLKYRLRHK EFEEIEGRLH RREPLILGAA
     ASQRLNRRLP VEVISDPLED LENGPYEDGC DAHKLRDHQV NDGRLRTAGE ASQRSTKEDW
     AEWMRHFSIQ LLKESPSPAL RTCARLAQLQ PFVGQELFAA GFVSCWAQLN ETSQKQLVRN
     LEMAFSSPNI PLEILATLLN LAEFMEHDEK PLPIDIRLLG ALAEKCRAFA KALHYKEMEF
     EGARSKKMDA NPVAVVEALI HINNQLHQHE AADGILTYAQ QHLDFQLKES WYEKLQRWDD
     ALMAYTAKAS QATSQHLVLD ATLGRMRCLA ALARWEELNN LCREYWTPAE PAARLEMASM
     AASAAWNMGE WEQMAEYVSR LDDGDETKLR GLGNTASGGD GSSNGTFFRA VLLVRIGKYD
     EAREYVERAR KCLATELAAL VLESYERAYS NMVRVQQLSE LEEVIDYRTL PIGDRVAEER
     RALIRNMWTQ RIQGAKSNVE VWQALLAVRA LVLPPMEDIE TWLKFASLCR KNGRISQARS
     TLVKLLQFDP EISPENVRYH GPHQVMLAYL KYQWSLGEDS KRREAFIMLQ NLAMELSSAS
     NIQPVTSSGF TNCLSPSVPL LARVYLTLGT WQWSLSPGLD DESLKDILDA FANATQYSNK
     WAKAWHKWAL FNTAVMSHYT LRGFPDIAAQ FVVAAVTGYF HSIACAANAK GVDDSLQDIL
     RLLTLWFNHG ATEEVQMALK KGFSLVNINT WLVVLPQIIA RIHSNNHAVR ELIQSLLVRI
     GQNHPQALMY PLLVACKSIS NLRKAAAQEV VDKVRQRSGV LVDQAQLVSK ELIRVAILWH
     ETWHEALEEA SRLYFGEHNI EGMLKVLEPL HEILEEGAMR NNVTLKERIF IEAYRQELLE
     AYECCVNYKR TGKDAELTQA WDIYYHVFKK IDKQLQSLTT LDLESVSPEL LECRNLELAV
     PGTYRAGAPV VTIASFARQL VVITSKQRPR KLTIHGSDGD DYAFLLKGHE DLRQDERVMQ
     LFGLVNTLLE NSWKTAEKDL SIERYAVIPL SPNSGLIEWV PNCDTLHHLI REYRDARKIT
     LNQEHKCMLS FAPDYDHLPL IAKVEVFQFA LDNTEGNDLA RVLWLKSRTS EIWLERRTNY
     TRSLAVMSMV GYLLGLGDRH PSNLMLHRFS GKILHIDFGD CFEASMNREK FPEKVPFRLT
     RMLEKAMEVS GIEGNFRSTC ENVMQVLRTN KDSVMAMMEA FVHDPLINWR LFNFNEIPQM
     SMLTSNHVTP AVNTEESAQN RELPYPQRGA RERELLQAVN QLGDANEVLN ERAVVVMARM
     SNKLTGRDFS TCSSVSNSSL QHAVDHNSLI SGDTREVDHA LSVKLQVQKL IDQAASHENL
     CQNYVGWCPF W
//
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