ID A0A2H3T833_FUSOX Unreviewed; 782 AA.
AC A0A2H3T833;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Phosphatidylinositol 4-kinase {ECO:0000256|RuleBase:RU367084};
DE EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN ORFNames=FRV6_08989 {ECO:0000313|EMBL:SCO84862.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO84862.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU367084};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU367084};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU367084};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367084};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU367084}. Vacuole
CC membrane {ECO:0000256|RuleBase:RU367084}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU367084}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|RuleBase:RU367084}.
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DR EMBL; FMJY01000005; SCO84862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3T833; -.
DR VEuPathDB; FungiDB:FOC1_g10010301; -.
DR VEuPathDB; FungiDB:FOC4_g10011893; -.
DR VEuPathDB; FungiDB:FOIG_08139; -.
DR VEuPathDB; FungiDB:FOMG_12458; -.
DR VEuPathDB; FungiDB:FOXG_08512; -.
DR VEuPathDB; FungiDB:FOZG_06723; -.
DR VEuPathDB; FungiDB:HZS61_012909; -.
DR OrthoDB; 1332545at2759; -.
DR Proteomes; UP000219369; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR039756; Lsb6/PI4K2.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR PANTHER; PTHR12865:SF1; PHOSPHATIDYLINOSITOL 4-KINASE TYPE 2; 1.
DR PANTHER; PTHR12865; PHOSPHATIDYLINOSITOL 4-KINASE TYPE-II; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU367084};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367084};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU367084};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367084};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367084}.
FT DOMAIN 162..577
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 88018 MW; B4CD3CCA739B80AB CRC64;
MPRSRPATTG YERLAQADDI SDDSDEDPLS QSYASLQPAA APRYAPVIQP RHRSGMASPK
SFASSSQPKF RHRSGSSAGV DLKAINARLE RWADEIASRF KRKGKNQQGE EERLEIHYSV
FQPPEGVRPV TAESIAAPQE GVMTRAEFET IVESVRSAIR QEIHPSMISQ GSSGSYFARN
PDGKIVGVFK PKDEEPYAAG NPKWNKWIHR NLFPCCFGRA CLIPNLSYVS EAAAYVLDCQ
LRTHLVPYTD VVWLASKSFH YPFWDRRKFH RKKKPLPAKP GSFQVFLKGF KDANVFLREH
PWPDQYWSGF RTNDGQSKKK RRWTESCRPS GNASPNDGYN SDDEEAAQAA NLLGPDNFIW
TDNLKESLRE ELEKLVILDY IMRNTDRGLD NWMIKVDWET GKASIASDPI QMNMEPVAEE
EGPRPVDLSQ QGPRATRASY PYKTQRPMSA SSRQPAGNEP AITIGAIDNS LSWPWKHPDA
WRSFPFGWLF LPVDLIGRPF SQKTRDHFLP LLTSTSWWTQ TILALKRVFQ MDVDFQERMF
AKQVAVMKGQ AWNVVETLKT PDHGPLELTR RARVCVWDDL VDVPVAVPMR NTSSEVRRNP
HARQSMDEAD IASSAPTNNP PIEDLLGLAS APADMPHPGR FELSSPTGET AQSPDEVPPS
EPNLLAPAGQ QQTGGDIAKR PTVQAAGFRN SYQGPVRALN MYEPARQQAP RQQRRYSFAN
AAARRNSNTI AQQYYGENEN YTDDLEGDLG YAAAEGQMGN QRKVIVERLE AVKSRNPVFT
CW
//
