ID A8Q6C4_MALGO Unreviewed; 2300 AA.
AC A8Q6C4;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=MGL_2920 {ECO:0000313|EMBL:EDP42720.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP42720.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP42720.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(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}.
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:EDP42720.1}.
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DR EMBL; AAYY01000010; EDP42720.1; -; Genomic_DNA.
DR RefSeq; XP_001729934.1; XM_001729882.1.
DR STRING; 425265.A8Q6C4; -.
DR GeneID; 5854241; -.
DR KEGG; mgl:MGL_2920; -.
DR VEuPathDB; FungiDB:MGL_2920; -.
DR InParanoid; A8Q6C4; -.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000008837; 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: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; 3.
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; 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:UP000008837};
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 1207..1761
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1937..2248
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2268..2300
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2300 AA; 260518 MW; 2F4C6F574EA27D9C CRC64;
MLSELKGERL QAFSNELNRR VIELTHSAQT ASKLGGITAI DNFIGLESED NSARLYRFYQ
YLKPNLPCSD PQVMFAAARV LGRVSKHGGH SLGDQFVEFE MQRALDFLQG ERNENGRYAA
VLIIKEMARN VPYLFHTYVG RVMDHIWVAL RDAKVAVREA AAEALGACFQ IISDREKQMG
TQAYELVYDD AEQGLRDTAV EVIHGSLLAI LKLLRYSKMF MKTRLHRTCE LILRLHRHRD
PLVKRTVTNL IPVLAAYDPP YYAQEYLGPV MTTLIDQLRR ERDRSTKEAW GDTLEAIGLV
SMAMGDRMQP YVDSIMQCVR ESLLLRGKKN MPPEGPVFFC LGHVALAVGT RIERDVHDML
DMMFACGLST ALVSALEKIV HAIPALLPIV QERLLMMLSY ILIGVPYRPL GAPLPRHGGR
PPPVLHVSPD AKTIETLTIA LQTLGSFDFS GHILNEFVRN CTLPYLELDA KDVRKAAAMT
CAHMYVNDPI CYQTSMHAIE VFNDVLDKLI MVGIADPDAE LRFTVLSALD EHFDRHLAQT
EYIRAIFIAL NDEEFAVREV AINILGRLAK YNPAYVMPSL RKVLIQLLTG LEYATVTRHK
EEAAKLLTGV VRALQGLVKS YALTILQVLL PKANDAHAGV AARVTECLGE LARVAGEELA
PLVDELVSLM VSQLSSGSVH ASVAKRDAAL KTLGRLASNT SHVANPYLQY PRLLGALVKI
LKTEQAAPVR RETIRVLGIL GALDPYRHKL LESTMDPVVT AGGSQTDLFE LATLIGTSTD
EYYQNVAIEA LIAILRDPTL SVHHHAVIEA IMYMFKTQGL KCVAFLPQIV PAFLGVIRTC
AGGGLSEFYY QQLAILITII KQHVRNYLRD IFALVQADWN PNSSIQLTIV ALMEAVARAL
EGEFKAYLPL LLPNLLQTLE GEITPKRMPT LLRMLQAFYV FGANLEEYMH LVLPVLVGLF
ERADAPMVLR RAAIVTVGQL SRKVNFADHA SRIIHPLVRV LQSGVAELRV PTLDTLTALV
FLMGPVYMPF VVVVNKAIVQ QRIQHPRYQQ VVAKLLRSEP LPLELLPPDT LALDKADEAP
HAEASKMAVN QLHLKAAWDT SRVSTAQDWR EWLRRVAVEM LRESPSHALR ACRSLAEVYH
PLALELFNAA FVSCWVELYD TYQESLVHAI ETALDAYEIP DQVVHILLHL AEFMEHDDKA
LPISIRLLGD RAYKFHAYAK ALHYKEAEFM AEPTPQIVEL LIDINTKLQQ GDAAFGALTY
AREHMDITHH EEWYEKLHRW EEALAAYERR ALEQPDAQEI VFGKMRCLHA LGEWEHLTEL
VQAKWPTAGP DGRRQMAPLA TAAAWSFGQW DIMDEFIAAM RPESSERSFY RAVLAVHHSQ
RHQTKRLIAR ARDALDTELT ALISESYGRA YDLMVRTQML SELEEALAYK LDYAEQPDRQ
ATMRTIWMKR LQGCELDVEV WQRILSVRSI VLTPADDMDT WIKFANLCRK SGRMVLAEKT
LNSLLGPEVH ALDSPLAGPK APPAVIYSHL KFMWACGARA ESLCYLRDFT MNLAEDLGMA
SVDKQDNLVL PDIRASPRLA EFAKLLARCF FKLGEWQVAM NEEWVVDDNY DVIRSYKRST
ELDRDWYKAW HAWALANFDV ITHHERHGVA IPFHEVAASI VPSVHGFFRS ISLASGNSLQ
DTLRLLTLWF KFGHLEHVAD AVRQGFSTVT VDTWLEVIPQ MIARISAPSP RVRRLIHHLL
SDVGTAHPQA LVYPLTVATK SPSPVRMHAA MGIMDTMREH SPVLVEQALL VSNELIRIAI
LWHEMWHEGL EEASRLYFTE HNIEGMFATL GPLHDLLERG PETLRETSFA QTHGRDLNEA
REYVRRYRQY GEINDLNQAW DLYYHVFKRI TKQLPASNSV QLALQYVSPK LLAMRDLELA
VPGTYVSGQP IVRITQFEPV VLVISSKQRP RRLKIRGSDG RTYQYLLKGH EDMRQDERVM
QLFGLVNTLL SIDTESYKRR LNLRRFPVIP LSPNTGMLGW VANSDTLHIL IKEYREQHKI
LLNIEHRLML QMAPDYDNLT VLQKVEVFEY ALDNTPGQDL YRVLWLKSRS SEAWLERRTA
YMRTLATSSV AGYILGLGDR HPSNLLLDRQ TGEIIHIDFG DCFEIACHRP KFPEKVPFRL
TRMLIKAMEV GGIQGTFKVT AENTMRVLRD NRESVLALLE AFVHDPLISW RLVTDSDAEQ
RAPDAHEHEH EVAGEIRGVE GEARNQRALE VVRRIQNKLT GRDFHPNISL SVPEQIERLI
QDATSIENLC VAFIGWCAFW
//
