ID S0EBY1_GIBF5 Unreviewed; 977 AA.
AC S0EBY1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=FFUJ_08633 {ECO:0000313|EMBL:CCT71307.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT71307.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000256|ARBA:ARBA00001686};
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DR EMBL; HF679029; CCT71307.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EBY1; -.
DR STRING; 1279085.S0EBY1; -.
DR EnsemblFungi; CCT71307; CCT71307; FFUJ_08633.
DR VEuPathDB; FungiDB:FFUJ_08633; -.
DR HOGENOM; CLU_002446_2_0_1; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000016800; Chromosome 7.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0005802; C:trans-Golgi network; IEA:EnsemblFungi.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:EnsemblFungi.
DR GO; GO:0006897; P:endocytosis; 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:2000786; P:positive regulation of autophagosome assembly; IEA:EnsemblFungi.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IEA:EnsemblFungi.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:EnsemblFungi.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 6.10.140.1260; -; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021601; Phosphatidylino_kinase_fungi.
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; IPR049160; PI4KB-PIK1_PIK.
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 Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR Pfam; PF11522; Pik1; 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 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCT71307.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..120
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 685..962
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 177..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 108393 MW; A4DA4D82DFD3DE9E CRC64;
MSWDLLQRFL ESDVFNSNPF LPVSYLSRYA DHVGIHYVLC QKLRQFPYED IEFFLPQLCH
LIISVHNESM ALEEFLMDLC EESVTAALLT FWLFQTYLHD LSSNPQSDSF QTCRRVYNKV
QHIVFGLADT ARHEKITENV LPVTVLSSFV LASIALPMFP QWAGPLAVAQ ARKPQPITNE
TQEPKENPKP TRARTVTVGN SRSRRVRDNG RTFSAPDPKG SRDSSPKPAR SPRPPSVIIP
PQRSKTQAGT TRPSALELRS LEAKLSTSSL PLPSAQPTTR PTTPNSAGNA QRPVENATRR
HSHHAKVVLT VSDMSPVQKT RLLRQHYFRS ETQFLTALEG ISNRLVLVPK PARMSALRAE
LALISQDLPA EIDIPVICPP TLVNGSPGKS RHHRIVRVNP AEATVLNSAE KVPYLIMVEV
LRDDFSFDPD QPENDRLLNS LLGGSARARR IFDLSDSPRL SPTVKAPEPL LDSVFEPASG
DLGSSPLLKG IDESPVRVSS RPAQNHTAQR LPSGATTSSS TLDLTTPRSS GTGTSRSNSP
GPVSRRMTMP IQRSAPADQP DFGALATHMR TASQMLAQLE ATSGKRPKQE VAAIRAKIIA
SMQSLEEKSF DVDEQGPTFD TIMAKASTTP IPVHNPDLEE DVQIDPNLNA SAGRERMEND
IKTGGVQRRG DRDDPSAAVF GEAWEAKKER IRKSSPYGWM KNWDLVSVIV KTGADLRQEA
FACQLIDVCH KIWVDAGTDV WVKRMRILVT GESSGLIETI TSGVSLHSLK RSLTLASVES
GQNPRNRIAT LRDHFLKAFG KPDSKEFQAG VDAFKKSLAA YSIISYVLQL KDRHNGNVLV
DSEGHIIHID FGFMLSNSPG SVGFEAAPFK LTHEYVDVLG GPLSPDFEDY KRLCKQAFQG
KLHQKYDVKN SMMGHDSRMP CFAVGIAQVT NTLRQRFQLH LSAEEAEHFV DDLVAKSFGS
YYTRLYDTFQ YRTQGIY
//
