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Database: UniProt
Entry: A0A225WKR5_9STRA
LinkDB: A0A225WKR5_9STRA
Original site: A0A225WKR5_9STRA 
ID   A0A225WKR5_9STRA        Unreviewed;      2658 AA.
AC   A0A225WKR5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE            EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN   ORFNames=PHMEG_0007605 {ECO:0000313|EMBL:OWZ18321.1};
OS   Phytophthora megakarya.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ18321.1, ECO:0000313|Proteomes:UP000198211};
RN   [1] {ECO:0000313|Proteomes:UP000198211}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA   Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA   Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT   "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT   of cacao black pod achieved similar genome size and gene model numbers by
RT   different mechanisms.";
RL   Submitted (MAR-2017) 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:OWZ18321.1}.
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DR   EMBL; NBNE01000605; OWZ18321.1; -; Genomic_DNA.
DR   STRING; 4795.A0A225WKR5; -.
DR   EnsemblProtists; OWZ18321; OWZ18321; PHMEG_0007605.
DR   OrthoDB; 8448at2759; -.
DR   Proteomes; UP000198211; 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:UP000198211};
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          1393..2022
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2200..2513
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2631..2658
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
FT   REGION          2482..2570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2510..2524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2658 AA;  296765 MW;  A6B08AEB8EC35597 CRC64;
     MADSFTRFLP GLRSSNSSVR HRAAQSLRHF IESESRDLSH GLYMKWVTDI SARLMLLCNS
     NENADRMGGI AAMDELVELF IAERNDQTII EFAHSLTKVF EKIPSADPPM LRVAAKALGH
     IVSTGGTSLI EFVEDYHVKP ALEWLKNETF HVRRHAAVMI LKELSINAPS TSFRYMDKYF
     DFIWSAFWDS KLVVRVSASE SLQTCFMLIQ QRESNRKTSW YNRALDEAES AFKRNSSDAT
     HGALLILNEL LRNTGDFMHS HYGRACRLVF SHQDHKSATV RSAVIGLFPR LAKFNTSVFV
     EKCYRPCMNH LLEVLFSATT TTRPDALLSI GKLSLAIGPL LARDEQALMA IMNGIKGGLQ
     VRKKDFDTHR EALACLRMLA ETVGPALIRV DLESMVGPLF QNDLDSSLVE TLTTIVKKIP
     PMKPIIQQKL FERLSSILRS RQNDVTGTAT TPTSRKLKAA SISVTGGMLS NLFLSATGSK
     ASSSENGAPS TEVSSAISMQ ALALETLANF DFQGNRLIPI MSFVHETVVK FLDHEVATIR
     KSAALTCCKL LLPQGEDRGG STAMTSEDFA RPVTSVLERL LTVGIADNEA SIRLRVLASL
     DSRFDPLLAL NDNLRCLFIA LNDEVFSIRQ TAMSTLGRLT HHNPSTVLPS LRQTLVQLLA
     ELEFSGDSRG KEEGALLIGC LLRSAAQLAQ PYVLPILRVL MKNLREDSER RSHSRSTVSV
     SKAILATLGD LAEVGAQELT PYLGQLLPDV IDEMRDSSNP QILQVAIKTL GQLVSSTGYV
     VLPYHEYPEL LDLLCQALQK SGDPFESLRI EAGRTLGVLG ALDPYNLRLF HLQKQGKLTD
     AKKKEFRSSA FAVGAGGVFS LMTNTTNPTE SLATNGFGSG SGAAKGAVIG IRIGNGIGGP
     GMLDGSSEED AQQLGESLLL TPARKVTKSD KQTSGKLTNI ILEVPPDDLL PSMIPDSSQY
     FPTVAINALI RILLEPRNSV HYQGTFMAIM YICKSQRKRM GQHLDKIIPA FLYALEKVNR
     SLRKFLFEQL CDLVQIVEEQ IQPHLDHVAL LSIISSYWDE HLEEVLNLVK KLANSLGENF
     RVYLPDLIPQ MLRVIRTERD NPARPRTLLV LKTAVSLGRL LDGYLHLIIP ALVALIQSDA
     DINARKQGLG SLGSLVKKLN VSVYASKIIH MLARVISSQP EMVYLAMDCL CCMVYTMGDD
     YAIFVPVISQ VLGRHTSRSN DIFDRYDLLV SKILKYQPLP VASWATDPLK SRVDTSSAHK
     DSSSSAQDET KSLPCDQKNL MKAWEASQRS TKEDWNEWIL AFSVELLRES PSPVLRACKE
     LASVYQPLAR ELFNASFVSM WPHLSSSTQD NLIRSLESAF QSPHLPSEIL QTLLNLAEFM
     EHDDQPLPID IRLLGSLADK CHSFAKALHY KELEFNTNPS TDGIQALISI NSKLNQPEAA
     RGILKYALEK LPGIEVKASW HEKLLRWDDA LATHDRVLQE DPSNVESIFG KMRCLWAIGE
     WRKLNDHVQQ TWTKIYGEGQ DLKREQVDGE KLLDVAPALK KELCSSGARV AFSLQNWDSI
     PKYINSDMDA TESHLFKAVV SIRRMELDEA MSSITDCRKE MDPTLRSLVS ESYGRAYLPA
     IVNLQMLTEL EEIVAYLKAF AYKNNGELTL LSTPVPSSTS MSTTASRRKQ SISSLNFVSS
     SSSTSYGHEK KVALKKLQTI WTRRMLGVER NIEVWQSLML VRSLVFDPRE DVDIWLKYAR
     LCLKSGHINL AASALWRVGA QPFIRSVERD PYTPIPINLG GNAGASQGFA NGLLSLADSA
     AQDPRVAFSY LRHLWAENRE DVALKQMDYF IEALEQHGDP TDEDMRKLRV QVYIQLGEWQ
     MSLNEQASGA YDHVLECLET ATKLDPTNDR AWHEWALMNF RALEATVKES GFGDPKRYAV
     RAIQGFFRSI SFGHTSYDVT KDVLRLLTLW FAQGNRSDVH TAMVEGFQDA SVDTWLDVIP
     QLIARIDTPN QKTSELLHDL LSRIGQAHPQ ALIYPITVAS KALNPTRKHA AEGILAAVRR
     HSSQLVYEAD MVSRELIRVA ILWNELWHGA LEEASKHFFN NRDVTAMIAE LAPLHEQMDQ
     IGTEETPTLR EVAFYQAFAR DLQYAKEWTN VYERTKSLDD LNQAWDIYYS VFSKIRKQLA
     NLSTLELANV GPKLLSVRGL TLAVPGTYKA GAPIVRIQSF DTKVTVLTSK QRPRRVAING
     SDGKAYPFLL KGHEDLRQDE RVMQLFGVIN TLLANDSDTS KRNLAIERYS VLPLSHTSGL
     IGWVPNCDTL HQLIRDYREA RKIQLNVEHR LMVQMAPDYD KLPLMQKVEA FKYALGETTG
     QDLYRVLWLK SQDSEVWLDR RRNFTRSLAV MSMAGYILGL GDRHPSNLML DRVSGKLVHI
     DFGDCFEVAM ERDKYPEKIP FRLTRMLTQA MEVSGIEGNF RYTCEASMRV LRDNRDSLMA
     VLEAFVYDPL INWRLLKKDA VPSHAQPEED DGAAGGGRGG AGAADSVDAH GHRNSSSAGN
     EDGNDTNGDG DDDNANGDNG DEDKLAEGSM KSSTSSAPRR RRHSSSEAML GYNMDMLDSA
     IARNSISETQ RDNFGTSFVA AEHPQLNEKA LSVVDRVKKK LAGRDFDDGS RVLTVDAQVD
     RLIHQATSHE NLCQLYYG
//
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