ID A0A1Y2W2Z0_9PEZI Unreviewed; 783 AA.
AC A0A1Y2W2Z0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Phosphatidylinositol 4-kinase {ECO:0000256|RuleBase:RU367084};
DE EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN ORFNames=M426DRAFT_321864 {ECO:0000313|EMBL:OTB03297.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB03297.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTB03297.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTB03297.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ111560; OTB03297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2W2Z0; -.
DR STRING; 1001833.A0A1Y2W2Z0; -.
DR InParanoid; A0A1Y2W2Z0; -.
DR OrthoDB; 1332545at2759; -.
DR Proteomes; UP000242955; 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 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; 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}; Kinase {ECO:0000256|RuleBase:RU367084};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367084};
KW Reference proteome {ECO:0000313|Proteomes:UP000242955};
KW Transferase {ECO:0000256|RuleBase:RU367084}.
FT DOMAIN 161..576
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 88722 MW; 4B342D551595541E CRC64;
MPRNRPATTG YERLAQADQF SDESDDDNLA QSTASLQPQS APRYAPITQP RPHSGMTSPK
PVSKPKYRPR RMRSNSGVDL KAINARLERW ADEIASKFKR GKGKGIPGEE ERLEIHYSVF
QPPEGVRPAT AETLATMPEP AMSRDEFEAI VDSVRVAIDQ GMHPSMITQG SSGSYFARNT
DGKIVGVFKP KDEEPYAAGN PKWNKWIHRN LFPCCFGRAC LIPNLSYVSE AAAYVLDCQL
RTHIVPYTDV VYLSSKSFHY PYWDRRSFHR KKKPLPAKPG SFQVFLKGFK DANVFLREHP
WPDQYWSSFR SNDTHRHKRK RWADNCRPTS RAARDNDSES EDERDAPEQR PLGPDNFMWT
ESLKQSFREQ LEKLVILDYI MRNTDRGLDN WMVKVDWTTQ AVSITSEPPQ LNMDIPEDEE
LPARPVDLPA RGKNQSRSPN PYKTQKPMNA SGRSKVPDPK MSIGAIDNSL SWPWKHPDAW
RSFPFGWLFL PVDLIGRPFS QKTRDHFLPL LTSTQWWSQT SLELRKVFQI DPDFQEKMFS
RQMAVMKGQA WNVVETLKTP DHGPLELTRR ARVCVWDDLV EVPVAVPMRA TSSDIRRKAE
SDTNKTIQEE MDIGAANSSS APAQVDLLGL TSPLPNPGRF ELTSSHEVSP DRTEPASEDF
TPTGVTQNPF DALSATESPS AGRPQIARGP RSSYQGPPRA QLNMYAPRKE RRYSFTTAAS
TPRNGNSIAA KLYANGNAYD EDEDDVDGDL GYAAAETMDG NRRKVIVERL ETVKARNPVF
TWC
//
