ID V9EGI2_PHYPR Unreviewed; 963 AA.
AC V9EGI2;
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=PI3K/PI4K catalytic domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=F443_15932 {ECO:0000313|EMBL:ETI38335.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI38335.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI38335.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI38335.1,
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 -!- 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:ETI38335.1}.
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DR EMBL; ANIZ01002770; ETI38335.1; -; Genomic_DNA.
DR AlphaFoldDB; V9EGI2; -.
DR EnsemblProtists; ETI38335; ETI38335; F443_15932.
DR eggNOG; KOG0903; Eukaryota.
DR HOGENOM; CLU_002446_3_0_1; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; 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 InterPro; IPR016024; ARM-type_fold.
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 PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 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; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 105..215
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 669..947
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 60..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 107693 MW; 7A0ADE2C1245192A CRC64;
MFRQNHQSKQ HKGAVLNHYI ICVCQRSPRL RATDLSVRMK ASTRSSFLFS RSSSKKLEID
EDERLHVQTG RGETAGQADD TKKELSTRGF ELSDVAAINA GEPNDRKIEG FLVFRKRMRQ
RRYCILQGDT MLVFKTKPSD SASPGVPKKQ ISVVGVKDAL ELEASVRVAL LGNGAADSYD
NTLVISSHKA KLVVIDTDTL TEKERWLHAM STIHVNSGDS EKNFFESILS ADTFDAQMAV
TLLHKYRSNA VATELVLDRL ASYAEENVDD VEFYIQQIVH LIVNTELVAT DKLVNLLLSI
CRAKAYVEHL GNCIHLALQL FWLLEAKIAD NDPKTYNLCA RLLMSIEAKV VNQHFEVPNT
QTAEDVTRRL MDIPQMREKL EQVSVDDTQG KEEVTGLAER LASELESSSA APLTPSKISS
QHALLLEWME KERKKRYKYF HEQRDFVKAL TDISERMRAV DPPQNRKKLL PGELKALVIP
DMAYVPLGRV SDSFCRITRV LPDEGTVFST HSRAPCLLCF EVIEDQVNSA GQRKLSTELK
NSCGLLHKSA SDPALANLEA EVASLVKKFA IKGQLICVEN PLSPHENEDD GADAEGGQDD
NGTADILESI DAPIFPLEGI RSGLSSPTST VLSDDSMDST SELSREGSQQ LNLIRGYSKT
AYEMGLSKLL SASEVFGESW EAKKERIRAS SPHGDLSGWN VISLISKSND DIRQEVFAMQ
LITTFQNIFR ESGLPLWLRP YRIVSTGRTS GLLETITDAQ SLDGLKKRSD YAGLRAHFER
TYGVGDDFKK AQRNFLHSLA AYSIVCYLLQ IKDRHNGNIM LDTEGYLVHI DFGFMLGIAP
GGNWSFETAP FKLTKEMVAV LGGVSSPLFG EFVQLVALGL LAAQRKSDRV VALVEIMMHN
STFPCFQGRD VSRDLQKLRS RFLLNYSTEK TVKAVVKMIR ASYKNKWTKR YDQFQKITNG
IIP
//
