ID A0A238F0W8_9BASI Unreviewed; 2396 AA.
AC A0A238F0W8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=BQ2448_5413 {ECO:0000313|EMBL:SCV67802.1};
OS Microbotryum intermedium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV67802.1, ECO:0000313|Proteomes:UP000198372};
RN [1] {ECO:0000313|Proteomes:UP000198372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (SEP-2016) 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; FMSP01000002; SCV67802.1; -; Genomic_DNA.
DR STRING; 269621.A0A238F0W8; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000198372; 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; 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; 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:UP000198372};
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 1275..1827
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2025..2336
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2364..2396
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2396 AA; 269102 MW; 6A878EC3211E3798 CRC64;
MSSSLLVAAK ASKAERPLDA ILGDLRSKHD EIRFKAAQEL YNYILASSRS LSAEAFNKTY
SEIHARCFAL VNSSDLQDKL AGVTAIDKIV DVLGNDMSRA IRLAASVQRA FPCSDSLVMT
NAAKVFARLA AQGGILMSGH VDTQVKSCIE WLQGDRIENR RYAAVLILRE LTRQAPGLIY
EHLTELLDNL WTAMWDPKVA IREAAADALA GCLLIATQRD GQLRVDAYNM VFGQAQIGFK
TGYPETIHGS LLGYKELFLE GKLFMADRYG EVCDQILFYK DHRDPLVRRA VIELIPTIAS
YNANEFAAHY LSRTMAFLLD QLKKDRGDRA TAFQAIGRVA LQVKSMMTPY LDPILNSIKD
GLLSRGRKNQ PAGLENSIFQ CIGMLAQSVG PALTKHMHEL LDLMFAYGLS PALHTALQQL
GRDIPPLLPD IQERILNLIS MTLADEPFVQ AGAPHKGSKH HDLTVNGVNG HHHHHPENQS
PERIMLALEV LGTFNFKGVF QPPRHLTPGM MPEPVVEQSL GEFVRDHVIH YVEDDNPDIR
RAAALSCCQV LSNDPIVTQA SNHAIKLMNE VLEKLLTLAI ADPDPSIRQA TISHLDPNFD
RHLAQADCVR SLFIALNDEV YAIRESAIRI IGRLATLNPA HVMPSLRKTL IQLLTELEYS
TASRNKEEAS TLLGLLVGAS QRLTKPYVTP MLKVLLPKSR DASPSVAASI VTTLGELTKV
GGEDVLPCLD DLMSLILDTL HDQASTQKRD AALRTLGQLA SYAGYVIDPY LQHPSLLGIL
ISLLKTEPAP HTRREVIRVM GALGALDPYR HSVVEGISND AYVESFNPTD PTHPSNIGPS
HEEYYPTVAF NALLGVFSDP SLSDHHTAIV DAIIYIFRSL RLKVVTFLPQ VLPVYLNVMR
TCPVGLQEFY FQNLSQLIQM VKQHVRNHLA PILAIVREFW NSTTNPGLQV IIIDVIQSIA
LALDAEFKAY LPNLLPLMLK AFEHDFVELR RQSSLIKVLH AFAVFGASLE EYLHLIIPAI
VSTFERPDIP AVLRRHAMQT ISQLCRKINF ADHASRIIHP LARVLANPAS PLELRVPAMD
AMCSLLLQMG PDFVLFVPMI HKILVRQRIS YPTYQTLVDK LLAEEPLPQD LTFGDPIIMP
NTEAIVAADA GMSKLPVNQV HLKSAWEIVD RPKADDWREW IKRISVQMLK SSPSLSLRAC
ANLAEVYHPL ARDLFNAGFV SVWGELYDNY QEDLVRAIQN AFSSPTLPPE ITQQLLNLAE
FMEHDDKVLP IPISTLGQYA LKCRAYAKAL HYKELEVLSD PSLHTIEELI RINNSLQQPD
VSVGILVHAH QRHGLVLKEE WYIELERWED ALAALQRKAQ EQPDSFDVTL GRMRCLHALG
EWESLAHLAQ ENWARASHDM KRKIAPMAAA ASWGLAQWES MDTFIGVLKH DSADRAWFRS
ILSIHRGQFN KAQSHINKAR DLLDTELTTL VGESYNRAYD AVVRIQMLSE LEEIISYKEA
SASGNLERRN LIQRTWMKRL LGCKRDVDVW QRILKVRALV VSPHENIEMW VKFANLCRKS
GRLGLADKTL NSLMPDDIGP GGAIGMTGPP EIIYAHLKYM WATGAREETL GFLRTFTSQR
SNEVGLTSNV LLPGNDSSSE SVSKDVRLLA RLYYKLGEWQ SAMQDDWGSD AITDILQSYL
LATKLDPTWY KAWHAWALAN SEVVSHYAKS LNEQDQIAPQ VFIDHLVPAV EAFFHSIALS
PGNSLQDTLR LLTLWFKYGG DEKVYEAIMK GMKTVSVDTW LDVIPQLIAR IHAPSANVRS
LIDSVLTDVG KQHPQALVYP LTVASKYPSA PRRSAAVAII DKMKVHSEAL VAQALLVSQE
LIRVAILWNE LWHEGLEEAS RLFYGDHNID AMFATLAPLH DMLERGPETL REIAFAQTFG
RDLADAREAC NRYRQFGEIQ DLNHAWDLYY QVFRKINKNL PTLTLLELQY VSPKLLAVKD
LDLAIPGEVW VRPGDTCLFL ELTPFLVVST GTYQTGKKIV RIASFGPTSE VFTSKQRPRK
LRIVGSDGVD YNFLLKGHED LRQDERVMQL FGLVNTLLQK DSETFKRHLT IVKYPVIPLS
PNSGLLGWVN STDTLHVLIK NYRDSHKILL NIEHRLILQM APDFDHLCLM QKLEVFEYSL
DNTTGQDFYR VMWLKSRNSE AWLDRRSNYC RTLAVMSMVG HILGLGDRHP SNLLMDRVSG
RIVHVDFGDC FEVAMQREKH PEKVPFRLTR MLMSAMEVSG IEGTFKITCQ HTMRVLRENK
ESIIAVLEAF VHDPLINWRL VQGGRQIEGK AAADSGGAGG ARRPRGDETN IYDEDAVDQI
NTRAVQVVER VQQKLTGRDF KPTVVLSVND QVDKLIAQAT SLENLSQCFI GWCPFW
//
