ID K5XEC1_AGABU Unreviewed; 2372 AA.
AC K5XEC1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=AGABI1DRAFT_35543 {ECO:0000313|EMBL:EKM81703.1};
OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS 10392) (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM81703.1, ECO:0000313|Proteomes:UP000008493};
RN [1] {ECO:0000313|Proteomes:UP000008493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC {ECO:0000313|Proteomes:UP000008493};
RX PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT "Genome sequence of the button mushroom Agaricus bisporus reveals
RT mechanisms governing adaptation to a humic-rich ecological niche.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH971387; EKM81703.1; -; Genomic_DNA.
DR RefSeq; XP_007327123.1; XM_007327061.1.
DR STRING; 597362.K5XEC1; -.
DR GeneID; 18829145; -.
DR KEGG; abp:AGABI1DRAFT35543; -.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000178_7_1_1; -.
DR InParanoid; K5XEC1; -.
DR OMA; CICVGAG; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000008493; 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 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:UP000008493};
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 1250..1807
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1981..2294
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2340..2372
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2372 AA; 269155 MW; 755373AAB1EEAD00 CRC64;
MAPNVQAPAE KLSTIFTGLK NRNADVRVQN AKELRRFVLT EVADMSSDAS VKIWDETINR
KLFELTHSQN TAEAYGGLMA IDYLLGTEPD ETIEAKRNLF RFYNYVKHLL PNHEVSLMLY
ASKTLGRIAE IGGSAFGERF MDYEVQAAID LIQPDKNESP RHAGVLILKE LARNSPTYFH
QHIDVVFENI LIPLRDPRVH IREGAAELLA ACLEIITTRE RQTRSPYFSK ILQDAHQGLK
GSSMDIVHGS LLTYRELLLH AGMFMKESYL DITEQILRYK SHRDPLIRKM VITMIPSLAV
YDTQTFTEHF LHKAMGHLLT QLEKPAERNY AFIAIGHTAN AIGSDMKPFL DSIMNQIKIG
LQGRGRKNAP NEEPLFQCMG MLAAAVGPNL TKLLHDQLDL MMSCGLSEPL KNALAIIAKH
IPPLLQTIQE DRLLDLLSQV LSGQPYKSLG APTPTVRQDN AGIMSNVPPQ ASHDKSPELI
TLALATLGSF DFNGHVLNEF VRNCAVPYLE DDQPEVRRAA ALTCCRLLVC DPICYQSSSH
AIEIISDVLD KLLTVGIADP DSSIRQTVLG ALHEKFDKHL AQAENVRSLF IALNDEVFEN
RMIAVGLIGR LAKHNPAYVM PSLRKALIQL LTELEYSTVL RSREECTRLL TLLVSCTQRF
IKPYALPILR VMLQKANDVN PTISANVLMC LGELVSIAGE DALIYVPDMM AIIIQRLSDP
SVIKRDAALH ALGQLCSSTG YVITPLVDYP QLVPLLSSIL RSDGAKNMRR EVVKVLGILG
ALDPYRRKVR STRPDDESMS EKVATAVNQV PAVQFNTVSG ADDYFQMVVI NALLAILKDQ
ALSSHHHTVI DAVMSIFKTQ GLKCVAFLPQ IIPAFTSVAR TASVARLQEF HLQQLAILVG
IIKQQVRNYM PEIFALITEL WEHSALQLPI VVLIEALGIA LDAEFKPFLP TILSLILKVF
EGGPPDDKRS SVQIKVFDAF LTFGSNIEEY LHLVIPIIVK TYERDGSTQL RKKAVQTING
LARSVNFSDH ASRIIHPLVR VLDNSNTELR ISVMEALCSL MMQLGADFAI FVPTINKSIM
RNKVVPHHVY ENMINKLLNG EPLPQDMALQ DSLEPNKITE FSAPAEASKM TVNQQHLKQA
WDVSLVATRE DWFEWIHRLS VEFMKESPSH ALRACMGLVD IHPPLAKELF NAAFLSCWSE
LYDQYQEDLV RSVEHAITSN DAPPELIHRL LNLAEFMEHE EKPLPIEHRT LGEYAMKYMA
YAKALHYKEL EYFSEASPAV VESLISINTR LQQHDAAWGT LITAKEQYNV TEHEEWYERL
GRWQDALVAY EKAADNDPSD LEVQYGRMKC LHALGEWEQL ATRVNEHWAT ASHDDRRDIA
PMAAAAAWTL NAWDDMEDYV NNMKSDSPDR AFYKAILFVQ QNQFPKALSQ IAKARDSLDP
ELSSFVGDSY GQLYGVMVRA QMLSELEEII AFKQYADQPE RQLTMRKTWL KRLQGCQPDV
EIWQRILQVR TLVLNPEDDP VMWIKFANLC RKNDRMPLAE KTINSLLSPE RVRLFDSFRH
HHTKATPNVV YAHLKYMWAQ GSREESLEFL RRFTEELAHD LSQEVGEPSH QLSMSISKQK
LTELSKLLAR CYYKQGEWQA KLGDDWGTRN TEDILHAYYL ATHYDATWYK AWHTWALTNF
EVVSELEAQA EGRTVDIPGE GIAAHVVQAV EGFFRSIALK NFDALQDLLR LLTLWFKFGA
HDDVSDAMAN GFSTVEVDTW LEVIPQIIAR IQTPSINIRR TISNLLTDVG KNHPQALIYP
LTVASKSSSV ARMKAAQAIM DRMGAHSPLI VNQAQSVSQE LIRVAILWHE LWHEALEEAS
RLYFTEKNPD GMMATLEPLH DLLEKGPRTA RETSFVQAFG RELHEAREAC RRFRNYGETA
ELDRAWDIYY GVFKRVDKQL PQLTSLDLQY VSPILLRSRN LELAVPGTYL SGRPIIRIHS
FTTKLTVITS KKRPRRLCLK GDDGRDYQYI LKGHEDLRQD ERVMQLFGLV NTLLSVDTNS
FKRRLHIQRY PVIPLAPNAG LLGTILDSDT MHVLVRDYRD SRKVLLNIEH RLMLQMAPDY
ENLTLLQKVE VFEYALSNTS GQDLYRILWL KSTNSEHWLE RRATYTRSLA VNSMVGHILG
LGDRHPANLM LVRSTGKLVH IDFGDCFEVA MHREKFPEKV PFRLTRMLTH AMEVSGIEGS
FRNTCEITMK VLRDNKDSLL AVLEAFVYDP LINWRLMQTE GEGRRNEGEE ISLDPDRAVE
VARVAVHPQG PQRRLGPNEN DIFNEAQGEP GAQEIRNERA LFVFHRVQHK LTGRDFNPEV
TLAVRDQVEK LIGQATALEN LCQCYSGWCA YW
//
