ID A0A225VXV2_9STRA Unreviewed; 1111 AA.
AC A0A225VXV2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphatidylinositol kinase {ECO:0000313|EMBL:OWZ09607.1};
GN ORFNames=PHMEG_00017663 {ECO:0000313|EMBL:OWZ09607.1};
OS Phytophthora megakarya.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ09607.1, 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 -!- 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:OWZ09607.1}.
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DR EMBL; NBNE01002725; OWZ09607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225VXV2; -.
DR STRING; 4795.A0A225VXV2; -.
DR EnsemblProtists; OWZ09607; OWZ09607; PHMEG_00017663.
DR OrthoDB; 69201at2759; -.
DR Proteomes; UP000198211; 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; cd00821; PH; 1.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR015433; PI_Kinase.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50003; PH_DOMAIN; 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.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OWZ09607.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198211};
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 35..137
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 197..252
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 824..1095
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 701..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 124323 MW; A070AE208B9867EF CRC64;
MADVDVDALL PETPVGAIAA LASRHKATAL TQPPPRLFGG YLRKRYSSSV YMGSWRFCVL
QGARLRWYRS KDCAETDTQL RGEVWVHSVE AWDGRAALSK YPHAFAVRTT GKKLLLCAAE
SARDREIWLK QLERALQRSK STAELLAAVP SDDGGRRIVP GDMRDPPPAP CGLDASIHSA
PSDLTYGQSL ALGDAGCAEC FVRFRPLVAR RVVCGSCARA FCARHCHHGV RLQHLGLRAA
RRCCDHCAQR QEFIGHLRAT KRFLTPMVSR GISMDALVAR SDAARNQGEM FARTLHKLRH
GPMTLNRTIK ILYQTRKKPH LFRVACERLP FYTETCVDRL ENLWYQLLHL VQCLDAEPAP
RCAAQLFYLQ RYIRAICRRC PRIALQTIWH VQASVGDGNY HNLHPHTLLS LLGFIYPNTT
LPESSRMFSV WKDLVYADCP EHQLAQILAD LREINADMEK LISLEPDSML ERWLNAKTLP
QFDCPEHQLA QILADLREIN ADMEKLISLE PDSMLERWLN AKTLPQFENC AAELAESGIE
LCEFQSSILY DSLDVEGSNV SDEVPGTDIE SLVLEQVSFV QSLAAISERL RHIQPVSDRG
KYLAGELETL NNTLKSSALY PLSAASDELY QVVRIPPTEG KVFSTKMRAP TLIFVETVPV
QSGSVGHDDT DTERLRPFVF SSHPRNSTFF ESAMEEIEAS AVSSSGETML SPYSSSTLAT
PTPTSAVPGP ASCPEDMIAL QASGVLDNDK ANERRPTGPG GIIGRHMTIP NGGREASASA
NGRRHTGIMP HLPQPSRASK MGAGARATRL GIENFVYDSK VFGESWEERK ARIQRESPMG
KLPGWNLFSV IVKTNDDLRQ EVFTMQLIHK LKSIFEFEAP HLWLRTYRIV ATGANIGLLE
TITDACSLDH LKKTFPGGNL SEYFRSVYGE PSRSEFIAAQ RRFIESMAAY SILSYVLLLK
DRHNGNILLS SEGRVIHIDF GFILGIAPGG MFSVEDAPFK LTKEMVDVMG GMGSPGYKRF
RRCLCEGFLV LQKYQSEIVA LLQTTGQHSP FPCFHGVKLA RVIIDLRTRL CVGLSRHEIR
YRVDHLLRKS YNAWGTRQYD SFQLRSNNIH P
//
