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Database: UniProt
Entry: V9EB15_PHYPR
LinkDB: V9EB15_PHYPR
Original site: V9EB15_PHYPR 
ID   V9EB15_PHYPR            Unreviewed;      2653 AA.
AC   V9EB15;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE            EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN   ORFNames=F443_17556 {ECO:0000313|EMBL:ETI36280.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI36280.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI36280.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI36280.1,
RC   ECO:0000313|Proteomes:UP000018721};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
RL   Submitted (NOV-2013) 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}.
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:ETI36280.1}.
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DR   EMBL; ANIZ01003046; ETI36280.1; -; Genomic_DNA.
DR   EnsemblProtists; ETI36280; ETI36280; F443_17556.
DR   eggNOG; KOG0891; Eukaryota.
DR   HOGENOM; CLU_000178_7_1_1; -.
DR   OrthoDB; 8448at2759; -.
DR   Proteomes; UP000018721; 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; 2.
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:UP000018721};
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          1391..2019
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2197..2510
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2621..2653
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
FT   REGION          2479..2560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2479..2493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2653 AA;  296981 MW;  357EE26C28A0C280 CRC64;
     MAESFTRFLP GLRSSNSSVR HRAAQSLRLY IESESRDLSH GLYMKWVTDI SARLMLLCNS
     NENADRMGGI AAMDELVELF IAERNDQTII EFAHSLTKVF EKIPSADPPM LRVAAKALGH
     IVSTGGTSLI EFVEDYHVKP ALEWLKNETF HVRRHAAVMI LKELSINAPS TSFRYMDKYF
     DFIWSAFWDS KLVVRVSASE SLQSCFMLIQ QRESNRKTSW YNRALDEAEG AFKRNSSDAT
     HGALLILNEL LRNTGDFMHS HYGRACRLVF SHQDHKSATV RSAVISLFPR LAKFNTSVFV
     EKCYRPCMNH LLEVLFSATT TTRPDALLSI GKLSLAIGPL LARDEQALMA IMNGIKGGLQ
     VRKKDFDTHR EALACLRMLA ETVGPALIRV DLESMVGPLF QNDLDSSLVE TLTTIVKKIP
     PMKPIVQQKL FERLSSILRS RHNDVTGSAS TPTSRRLKTT SISVTGGMLS NLFLSATGAK
     TNGTAENGAP SAEVSSAIAM QALALETLAN FDFQGNRLIP IMSFVHETVV KFLDHEVATI
     RKSAALTCCK LLLPSGEDRG GNMAMTSEDF ARPVTSVLER LLTVGIADNE ASIRLRVLAS
     LDSRFDPLLA LNDNLRCLFI ALNDEVFSIR QTAMSTLGRL THHNPSTVLP SLRQTLVQLL
     AELEFSGDSR GKEEGALLIG CLLRSASQLA QPYVLPILRV LMKNLREDSE RRSHSRSTVS
     VSKAILATLG DLAEVGAQEL TPYLGQLLPD VIDEMRDSSN PQILQVAIKT LGQLVSSTGY
     VVLPYHEYPE LLDLLCQALQ KSGDAFESLR IEAGRTLGVL GALDPYNLRL FHLQKQGKLT
     DAKKKEFRSS AFAVGAGGVF SLMASAANPS QAYAGPNAAK ETNGAVIGIR IGNGIGGPGV
     LDGSSEEDVQ QLGESLLLTP ARKVAKSDKQ TSGKLTNIIL EVPPDDLLPS MIPDSSQYFP
     TVAINALIRI LLEPRNSVHY QGTFMAIMYI CKSQRKRMGQ HLDKIIPAFL YALEKVNRSL
     RKFLFEQLCD LVQIVEEQIQ PHLDHVALLS IVNSYWDEHL EEVLNLVKKL ANSLGEKFRV
     YLPDLIPQML RVIRTERDNP ARPRTLLVLK TAVSLGRLLD GYLHLIIPAL VALIQSDADV
     NARKQGLGSL GSLVKKLNVS VYASKIIHML ARVISSQPEM VYLAMDCLCC MVYTMGDDYA
     IFVPVISQVL GRHTSRSNDI FDRYDLLVSK ILKYQPLPVA SWATDPLKAR ADTANDHKDS
     NSAAQDETKS LPCDQKNLMK AWEASQRSTK EDWNEWILAF SVELLRESPS PVLRACKELA
     SVYQPLAREL FNASFVSVWP HLSSTTQDNL IRSLESAFQS PHLPSEILQT LLNLAEFMEH
     DDQPLPIDIR LLGSLADKCH SFAKALHYKE LEFNTNPSTD GIQALISINS KLNQPEAARG
     ILKYALEKLP GIEVKASWHE KLLRWDDALA THDRVLLENP NNVEAIFGKM RCLWAIGEWR
     KLNDHVQETW SKIYGEGQDL NGEQEDGEKL LDVPPALKRE LCSSGARVAF SLQNWDSIPK
     YINSDMDPTE SHLFKAVVSI RRMELDEAMN SIGDCRKEMD PTLRSLVSES YARAYLPAIV
     NLQMLTELEE IVSYLKAFAY KNNGELTLLS TPASSTSMST TASRRKQSIS SLNFVSSSSS
     TSYGHEKQVA LKKLQTIWTR RMLGVERNIQ VWQNLMLVRS LVFDPREDVD IWLKYARLCL
     KSGHINLASS ALWRVGAQPF IRSVERDPYA PIPINLGGNA GASQGFANGL LSLADSAAQD
     PRVAFSYLRH LWAENREDVA LKQMDYFIEA LEQHGDPTNE DLRKLRVQVY IQLGEWQMSL
     TEPHKQSYDH VLECLETATK LDPTNDRAWH EWALMNFRAL EATVKESGHG DPKRYAVRAI
     QGFFRSISFG HTSYDVTKDV LRLLTLWFTQ GNRSDVHMAM VEGFQEASVD TWLDVIPQLI
     ARIDTPNPKT SELLHDLLSR IGQAHPQALI YPITVASKAL NPTRKHAAEG ILAAVRRHSS
     QLVYEADMVS RELIRVAILW NELWHGALEE ASKHFFNNRD VTAMIAELAP LHEQMDRIGT
     EETPTLREVA FYQAFARDLA YAKEWTNVYE RTKSLDDLNQ AWDIYYSVFS KIRKQLANLS
     TLELANVGPK LLSVHNLTLA VPGTYKAGAP IVRIQSFDTK VTVLTSKQRP RKVTINGSDG
     KAYPFLLKGH EDLRQDERVM QLFGVINTLL ANDSDTSKRN LAIERYSVLP LSHTSGLIGW
     VPNCDTLHQL IRDYREARKI QLNVEHRLMV QMAPDYDKLP LMQKVEAFKY ALGETTGQDL
     YRVLWLKSQD SEVWLDRRRN FTRSLAVMSM AGYILGLGDR HPSNLMLDRV SGKLVHIDFG
     DCFEVAMERD KYPEKIPFRL TRMLTQAMEV SGIEGNFRYT CEASMRVLRD NRDSLMAVLE
     AFVYDPLINW RLLKKDAVPS HAQPEEDDGA AAGRGDGPDA SVDRNSVRED EGDADGEGDV
     ANGGNADEDK LTEGSMKSST SSAPVTPRRR RHSSSEAAML GYNMDMLDPT MARNSMSETQ
     RDNFGTSFVA AEHPQLNEKA LSVIDRVKKK LAGRDFDDGS RVLTVDAQVD RLIHQATSHE
     NLCQLYYGWC PFW
//
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