ID W2LG85_PHYPR Unreviewed; 1071 AA.
AC W2LG85;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Atypical/PI3K/PI4K protein kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=L917_06555 {ECO:0000313|EMBL:ETL95689.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL95689.1};
RN [1] {ECO:0000313|EMBL:ETL95689.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL95689.1};
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 CHvinca01.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI678989; ETL95689.1; -; Genomic_DNA.
DR AlphaFoldDB; W2LG85; -.
DR EnsemblProtists; ETL95689; ETL95689; L917_06555.
DR VEuPathDB; FungiDB:PPTG_21000; -.
DR Proteomes; UP000054423; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 48..150
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 218..273
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 783..1055
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 682..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 119149 MW; F2900C3A9A33D7A4 CRC64;
MPGASATMTE PPAVDVDALL PETPVGAIAT LTSARDKAQA LTHAQHPPRL FGGYLRKRYS
SSMYMGSWRF CVLQGARLRW YRSKECAETD TQLRGEVWVQ SIEPWDGRTA LATYPHAFAV
RTTSKKLLLC TAETQRDRDL WLQHLERALQ PSKSTAELLA AVNSDEGGRR IVPGDMRPPP
TPCAFQERPA AGSDATSIRS APSDLTYGQS LALGDAGCAE CYVRFRPLMT RRVLCGSCAR
AFCARHCSHG IRLQHLGLRA ARRCCDHCTQ RQEFIGYLRS TKRFLGPMVS RGISMDALVA
RSDARNQTGD MFARTLHKLR HGPMTLNRTI KILYQTRKKP HLFRVACERL PFYTETCVDR
VENLWYQLLH LVQCLDAEPA PRCAAQLFYL QRYIRAICRR CPRIALQTIW HAQASVGDGN
YHNLHPHTLL SLLGFIYPNT MLPESSRMFS IWKDLVFADC PEHQLAQILA DLREINAHME
KLISLEPDSM IERWLNAKTL PQFENCAAEM AASGIELCEF QSSILYDSLD VDSSNLSDEP
PGTGIESLVL EQVSFVQSLA AISERLRHIQ PVSDRGKYLA GELETLNNSL QSSALYPLSA
ASDELYQVVR IPPTEGKVFS TKMRAPTLIF VETVPVQSAG VIGLDDTDTE RLRPFVFSSH
PRNSTFFESA VLDEIETSAV SSSGETMLSP YSSSTLATPT PTSTAAGPVT CPDDGAPMQA
SGAGSEGTIG RGRDAAAPAS GRRHTGIMPH LPQPSRGSKM GAGARAGRLG VENFVYDSKI
FGESWEERKA RIQSESPMGK LPGWDLFSVI VKTNDDLRQE VFTMQLIHKL KSIFEFEAPH
LWLRTYRIVA TGANIGLLET ITDACSLDHL KKTFPGGNLA DYFRSVYGSD TLSSEFIAAQ
RRFIESMAAY SIVSYVLLLK DRHNGNILLS SEGRVIHIDF GFILGIAPGG MFSVEDAPFK
LTKEMVDVMG GLGSHGYKHF RNCLYEGFVV LQKYHSEIAA LLQTTGQHSP FPCFHGAKLA
RVITSLRTRL CVGLSRRDIR HRVDQLIRKS YNAWGTRQYD SFQLRSNNIH P
//
