ID H3GL97_PHYRM Unreviewed; 1373 AA.
AC H3GL97;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Phosphatidylinositol 3-kinase {ECO:0008006|Google:ProtNLM};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra77130, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra77130}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra77130};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
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DR EMBL; DS566019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 164328.H3GL97; -.
DR EnsemblProtists; Phyra77130; Phyra77130; Phyra77130.
DR VEuPathDB; FungiDB:PSURA_77130; -.
DR eggNOG; KOG0904; Eukaryota.
DR HOGENOM; CLU_261661_0_0_1; -.
DR InParanoid; H3GL97; -.
DR OMA; MFQLQEV; -.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00821; PH; 1.
DR CDD; cd00891; PI3Kc; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR035448; PI3Kc.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF14; LD28067P; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 169..276
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 281..379
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 462..631
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 657..771
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 830..1008
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1081..1358
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1373 AA; 155845 MW; 98FA6E1EBDA17A50 CRC64;
MFSLNPRQSM QSVLNGGGSS ASSMRSSTAS SFISAAYNSY ESGASFRNVD VSLVPSFEAL
NPYAKVGRSM MGDDKRWQPV PDLYHSKESL YFRSAVGKVL KIAHEEISPA ELEVRANTPE
FKVEEGDWIA HNSNQKNQFA LITPLKTVAR IPANLIISDE PISLTQHLSN HMGGYLRKKG
EKNKAFKKRY MELNGSVLAY FKKKPEKNGI PLSRDEKKTL ERGRIDLDRV SSLQPMESKS
EPYGILLVTT ARTWAICADS EPEYQRWLKG LCDVVKFSAV HVTYKRMFQL QEVSAKAITD
VRMVVTTGDT VGQIVEHIFN CYEQALDAAP LRPYNPAEYR LKITGYRDYM IDRFRVLNEY
VHVRECLLTK KTIRLTVIHE SVIQETAMMN LTIGRDLPVS TGSMNNIVNQ FADMFDGERS
TSLQMTTLGD EWERQSVDRN PSLPSGIVQQ PFAIRIRRVL NIPRTTCVRK RSSEEAVVSR
IPLTSSSVIV RIELFDGGQL LENAVIDTSD VRLKAQRNDL LYAEWEDSLW HKFNIDICNV
TRTMRVQLTV LGVKKVVGNS AANMDATEEK MLVTGVNAFD VDDTLTQGQQ YVHMYNNLHS
CVQGPVPHVT LPNEPMIQVE LSKFDSPIKF DWSDDDESVA SDRSHRRSII TSSRSVMLRK
EGWLQKVGNF SSLTRWRRRW FVVDQSTCTL SYADDETAPR KLITLRNCSV TTADDMNQKF
TTAPVNKGTR KLRQTWCFKV RPMGSSRDYI ISAETKQDRE EWMLAISTVA KGDSSFNDFG
SSNGSFEESS ASLSIPAESP RAEESNDQLD GRNILESVAQ DRRDSTSRCS GHSSTQRESE
LNELRKLILL DPLYRFSPYQ KEQLWMHREE FIDIPAALPR ILSCVHWDDR DECEEALKLL
PRWSVPDHQA AYIEFLNGEF AHEGVRSFAV QKLSQMADTT FSYFLPQLVQ AIKFENHHVS
PLAMMLIERA IKNPNQIGFD LFWSMKVEAH NDQYRERYGT ILNAYLDVCS SKMRAILKLQ
DKLFSEGGML ERICQSVKAK KKDGAAEMKR AMQQGLEALN ELLPGSFQLP LDPRIEVGKI
IVSKCRVMDS AKKPLWLVFE NAEEGGDPVT VMFKAGDDVR QDCLTLQLIR LMDEMWRDEG
LDLAMEPYKC VATSPMTGIL QMVPNSVTTA EVHRRDGMMG TFKDPSFSDW IRANNPDGRS
HKAAVDLFGR SSAGYCVATC VLGIGDRHND NIMIASSGRY FHIDFGHFLG HLKYYKLGIR
RERTPFVFTN EMAYVLGGVE GKDFGKFVDT ACTAYCVLRR HMHLLVSLLL LMVPADMPEL
TGRDDINHIV TTLAPEVSDE RARESFEQTI HFCLDSRFKR FDNYLHNIAH AFG
//
