ID A0A0W8CBB0_PHYNI Unreviewed; 1024 AA.
AC A0A0W8CBB0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=phosphatidylinositol 3-kinase {ECO:0000256|ARBA:ARBA00012073};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
GN ORFNames=AM587_10016537 {ECO:0000313|EMBL:KUF81342.1}, AM588_10011272
GN {ECO:0000313|EMBL:KUF93484.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF81342.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, Race 0
RC {ECO:0000313|EMBL:KUF81342.1}, Race 1 {ECO:0000313|EMBL:KUF93484.1},
RC and race 1 {ECO:0000313|Proteomes:UP000054636};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KUF81342.1}.
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DR EMBL; LNFO01004205; KUF81342.1; -; Genomic_DNA.
DR EMBL; LNFP01000382; KUF93484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8CBB0; -.
DR STRING; 4790.A0A0W8CBB0; -.
DR EnsemblProtists; KUF81342; KUF81342; AM587_10016537.
DR EnsemblProtists; KUF93484; KUF93484; AM588_10011272.
DR OMA; IRDHGTI; -.
DR OrthoDB; 11111at2759; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR Proteomes; UP000054636; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00896; PI3Kc_III; 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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KUF81342.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 144..185
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 382..568
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 693..961
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 24..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 115859 MW; F2193A1E5CCFCF7F CRC64;
MYSNDTSRDA AAVDLSFSQI LEARSTLHQQ QRRRRKPPVA NGQLQRPANQ QVRRFPPPPP
GTPSTFLENE DNAPPAYGNG MLDSVYEGSE DILEESEEEV RAGVSIHMGS SMDDEDWTNG
DDGQLGQDMY RFVQPRRLSS WVQDDAVFAC FKCHTVFSLL IRKHHCRACG RIFCSACSSQ
RVVIPGDYEA TPVAPAYNSL TTNASDLIGN ISWYLTSYSS PNAASGVDMN GSMSIRHSQS
FVDSGTLTPE EQQEKFLKDV QRLQENSVIS KFTPNRSRSG SASSTGTTAS SSHRSMHVPD
GSVMQRVCDD CACALQQRRH HYNTVKVFEL CEFNLQELRT LGQVCRKWHR ATIMCLSMFR
QIQYYLPTHR LSEREKKMLI INRKFLGGHT KWLLQLVKAV DFSEENELEH LVTNMTESEV
EGPASARRRH ERNSKLIDEV LELLQQERKH KCMLTMCSRL CKPQIGSVDA LEILADETIH
NHRLRAMAVD ALLKTATENE WWSYLQVLLH SLSVETNAAG SKLGQSLLRQ AQCDIRFCYD
LYWGLTVMAE DPSCRRKFDG MKQRLLLTLA QFKDKSSNGS LVESRKFASD DIAEQLLRGQ
ELVDLMWKIP PRIPVDDVRR ILEASIKKSS LGSSTDERKA GDQTPANDEQ EWRLLRLPVD
PQVKVSGINY QKIEVKRSAE APMIITCTGV DRDEEAEDTA DASTESQRNT WSRRTQKLPH
YRLMYKRDDL RKDSIVQNII NVMYLILKQE TRLDIPLVTY RVLPTSSFDG LIEIVENAHT
LYSIIRDHST IMNFLHHYNG HRTLSDISSS FRESLAAYTV ITFLLGVGDR HADNVMLTKD
GILFHIDYGF ILGKDPKPLQ PPMRLDHYMI EALGGTQTPQ FEQFKQLCVI AFNCLRRHVS
LFMIMLTLVV KALPEITDFG VNYTQSDLEA FVIERFLPGQ SDDEAATALM LRMEGKLNER
IGMKLSDFVH AHSNEKTVSK GMTSVGSSVK IGVEAVEATV STVASSLTSG ASSIYKYMWG
GPER
//
