ID J4KQD6_BEAB2 Unreviewed; 1947 AA.
AC J4KQD6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=BBA_02054 {ECO:0000313|EMBL:EJP69019.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP69019.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP69019.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP69019.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR EMBL; JH725153; EJP69019.1; -; Genomic_DNA.
DR RefSeq; XP_008595373.1; XM_008597151.1.
DR STRING; 655819.J4KQD6; -.
DR GeneID; 19885066; -.
DR HOGENOM; CLU_000893_1_0_1; -.
DR InParanoid; J4KQD6; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:EnsemblFungi.
DR GO; GO:0061909; P:autophagosome-lysosome fusion; IEA:EnsemblFungi.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:EnsemblFungi.
DR GO; GO:0140504; P:microlipophagy; IEA:EnsemblFungi.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IEA:EnsemblFungi.
DR CDD; cd05167; PI4Kc_III_alpha; 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 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; IPR045495; PI4K_N.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF15; PHOSPHATIDYLINOSITOL 4-KINASE ALPHA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF19274; PI4K_N; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1369..1555
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1668..1931
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1947 AA; 217874 MW; 0FEBDC9385533305 CRC64;
MTGGIRARAL DKIASLAASS TNTSFDKSDL DRLCRACNAG GRSREYNHGA YNSKQAGSLG
RIPMSIREFE VLLALCKNAP HVLSPQSAQK LSYQLIPYIL EAHSQTFVPS PFFRKVKPCP
TESLSFHVTA ALLALGINYN ELKETVTDGI WAFTNACSRT TESVLSPRTG DPENLNIDEA
IRTLNIAVAI LGFLDAAAAQ ADFWRAGGRL GLIQKAKQLL SEPFLVAVET ALSTIRNAHS
DDRDVREWKR HLRHYSAAGR PLGAMLLQRS FMWLVLSSTS LMIADGSQLR KKHVLDVLME
NGGILPRVDG FSPDADLRSI DLHANIAIDQ MNYIEAGADF ARLGSPSQQK LAYAVKSAAM
ISFLNCSMVN EDAAEPELLM NWLQQTLDDP QQMSDETLAS TTFRCMALLS RISPSFSQTV
IRSLPRFIVQ DVTNANTGAV AARSLAFVLK KLSKDAVIST LYSLGNVLSP DTQARLVNGH
TNGSVDGENG LNPVYQRRHS NASTISVNMS GEEEAAIVYR NVVQAICGIA TACEDEKITA
LAQSILLQKL DKVNTIVDVQ VIYGAADLAL SGGQLEFRSL LKMYNRLGHF GVTEQKEFYS
QAVLKGRTHI SANLRRDSPL FDIYWEHLLD SIIALGDAYS QGQTKQVDVD LAAQEIGELL
HPLAVLMSAN DLAARPLEND ESYALLRDAW FNIVVHGFST STERGKRYIN ELRMIAIHSP
PLAAEQRGEQ VESDIELNTV LRRGNSGDRD SMQKKLLTEL IPSKASDIKS LSYRKVIFLH
SAYLVEILRA DSGDCTKVLS YFAERSMLQR EVGSVMEGIT NAVVDKYIKK TISGVETAFS
AQYAAKQLAT IFSLCCHRIE RVQKAAFASA DKIVRDVPSS LCYRTSLFAL LELLSLMWSS
CLEAETDMYG HRSTFTSERG NVTVRLSDDY DFRSLTLKHL HQRARAWVSA SINLAPLDVK
GLLQTYLSEF DDEGTYGHIS LGRSFALELG SSIPNTDNRL QSLDQIGEYG INSASDLIAQ
YTTRQEYRYG ETLSDRGTEL MSFVQSNRRP SFSQSSVVES ANAATALAHV EARILSKKAT
PIDEVRDIMR RAAGLLCRSK HDESAVARYL VSIPFALFTK QSIKLGSSLW LGVMNENPRL
ESKLLNAIAQ QWEFTISRRV GLFDPSLEHP DPFFLKQEFS PSDWEMINQQ KQKVHDMLSP
HTRLLQFFSS HFNATRLGSP DIQRVFLRML DLTLAALKDC SPHPMAREIR FQIILFSTKV
LRNSTTIGPT AQWRLKDRIL SAGLSWFRHS PRWSFGSNML SLKTEIRLLS DVLASLNLVA
HIGSHTVGNV ISLQSKDSLL KVLLENEQSR LIVWANPRNL SGTRFPTHHS SKHATENALL
PLVRTAWHQD PSIAVELATR FQYPRLRSDV RRLILASPEK VIDEPEAIPL MIGSSLPDDV
NSQLKYLLFW EPVNPITAVT LLSPAFGDHP FIIQYAMRSL ESHSVDVTFF YVPQIVQSLR
HDNLGYAERY ILETAQFSQL FAHQIIWNMK ANSYKGDDAE VPDEIKPTLD NVMVKMVDSF
MPEDRTFYER EFSFFDEVTG ISGKLKPYIK RPKPEKKQKI EEELMKIKVE VGVYLPSNPE
GVVIGIDRKS GKPLQSHAKA PYMATFRVRK NRHAGDIPLE DVEDKQVVKQ QPPTKQQAVE
PQDNYIEVWQ SAIFKVGDDV RQDVLALQMI SAFRSIFHNV GLDVYVFPNR VTATGPGCGV
IDVLPNSISR DMVGREAVNG LYEYFRAKYG NEDSLRFQAA RSNFVKSMAA YSVISFLLQF
KDRHNGNIMI DDAGHILHID FGFCFDIAPG GIKFERAPFK LTSEMVAVMG GATDHQSFQQ
FEELCVKAFL AARQYRDKLA QVVQLMMDSG LPCFKPESVK HFKDRFVLDK TEREAADFMR
DLVKKSHSSY STGIYDQFQL LTNGIPY
//