ID W9YJT2_9EURO Unreviewed; 779 AA.
AC W9YJT2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Phosphatidylinositol 4-kinase {ECO:0000256|RuleBase:RU367084};
DE EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN ORFNames=A1O3_06337 {ECO:0000313|EMBL:EXJ82524.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ82524.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ82524.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ82524.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ82524.1}.
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DR EMBL; AMGY01000005; EXJ82524.1; -; Genomic_DNA.
DR RefSeq; XP_007734647.1; XM_007736457.1.
DR AlphaFoldDB; W9YJT2; -.
DR STRING; 1182542.W9YJT2; -.
DR GeneID; 19170447; -.
DR eggNOG; KOG2381; Eukaryota.
DR HOGENOM; CLU_009049_2_0_1; -.
DR OrthoDB; 1332545at2759; -.
DR Proteomes; UP000019478; 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 Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367084}.
FT DOMAIN 161..575
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 88386 MW; CE3CC6F2B4F7B0F2 CRC64;
MPRHRPTSGY ARLAQADDDD GPLADDDSGD EIYNNTPLST RYASIQPGPR ELMRSRPYHD
RRRATRRTRS NSSGVDIKAI NARLERWAEE IASKFKINSV RGKTHEEEHL EIHHSVFQAP
PEVRPYTAAD LAAYEAADTQ RMGKAQFDAI VESVRVAMEQ GVHPKMISQG SSGSYFARNS
QGKVVGVFKP KDEEPYASRN PKWTKWIHRN LFPFFFGRAC LIPNLSYVSE AAAYVLDCQL
RTNLVPYTDV VWLSSKSFYY DFWERRSTWG GKKSLPAKVG SFQVFLKGFK DANIFLRENP
WPDQATEFRS DLEHTRQRRP LSNCFPVRGQ PSDNDGGTPA VMSPQLEEQT PKFHWTPRIK
QAFREELEKL VILDYIMRNT DRGLDNWMIK IDWKTEEVSL VVEPPKENGT ARDGDTTTQS
KSVSPARPES NTSRPYRRYE TMESRSGTPS NARDDSHLTI KLGAIDNSLS WPWKHPDAWR
SFPFGWLFLP VSLIGQPFSK KTREHFLPLL TSTAWWSQTQ LALRRVFALD ADFKESMFAR
QIAVMKGQAW NVVETLKQED HGPLELTRRT RICVWDDLVD VPVAIPLRVP SAEMSRRKHH
HYDQQEEMDI GASYSSAPSG RQASQPDLLG SLTPDLPNPN RFELTREDGG ADLSYLAGEE
GPVSPVSGGP FFDAADYAKE ARNSLGNSAA TLPARPTAKS RNRLSFEFPR RETTSKSSSR
RQRSLSTRSG KSPAILYEGD DLEGDLGYAA ASDMEQNKRK VIVERLETVK SKAPVFTWC
//
