ID A0A175W916_9PEZI Unreviewed; 839 AA.
AC A0A175W916;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Phosphatidylinositol 4-kinase {ECO:0000256|RuleBase:RU367084};
DE EC=2.7.1.67 {ECO:0000256|RuleBase:RU367084};
GN ORFNames=MMYC01_203634 {ECO:0000313|EMBL:KXX80288.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX80288.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX80288.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-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}.
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:KXX80288.1}.
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DR EMBL; LCTW02000064; KXX80288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175W916; -.
DR STRING; 100816.A0A175W916; -.
DR VEuPathDB; FungiDB:MMYC01_203634; -.
DR OrthoDB; 1332545at2759; -.
DR Proteomes; UP000078237; 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:UP000078237};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367084}.
FT DOMAIN 166..579
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 93412 MW; FCD6C3EDDB3D81B7 CRC64;
MPRSRPATTG YERLAQADQF SDDSDDDPLA ASYASLQPAA APRYAPISQP RPHSGMATPK
GSGRRSSSGP ANRHRRRSRR NSGVDLKAIN ARLERWADEI ASKFKRGRNK KRGEEERLEI
HHSVFQPPEG VRPVTAEMLA VPEPGYMTKA EFEAIVESVR SAIRQGVHPR MISQGSSGSY
FARNPEGKVV GVFKPKDEEP YAAGNPKWNK WIHRNLFPCC FGRACLIPNL SYVSEAAAYV
LDAQLRTHMV PYTDVVYLSS KSFHYPFWDR YNFSRKKKAL PAKPGSFQVF LKGFKDANIF
LREHPWPDQY LSGFRTSDPH RKRKRRWADS CRPSSAQPDD GDSDDDHDTP HSLTPGPDNF
VWTPTLKQAF REELEKLVIL DYIMRNTDRG LDNWMIKVDW ETEAVSVASE PVRLNMDTED
PEEGPRPVDL AQRGPAKTRA SYPYRVERPM NASAPASGTP DPKISIGAID NSLSWPWKHP
DAWRSFPFGW LFLPVDLIGR PFSQKTRDHF LPLLTSTQWW SQTQLALRRV FQLDPDFQER
MFARQIAVMK GQAWNVVETL KTPDHGPLEL TRRAKVCVWD DLVDVPVAVP MRVASAEMRH
RAAAESDSAA AAATSHHGHK DKDRAHSDMI AEAEEMDIGA ANTSGDGKAS SAPATAGAGA
GAVVDLLGIT SPPADLPHPG RFELAMADEL PSSSPLSNAN GAAGALARPD IVVSDGTPTR
PQFNRASHSH RTLNMYSPER GDRPALADHE RRFSFATAAS RRESNSIAAQ LYGGRSSHDY
GLDHRHRQDG WADDDEGEDD LEGGDLGYAA ATGMEGNQRK VIVERLEPVK SRNPVFTWC
//
