ID A0A1V8SSF5_9PEZI Unreviewed; 762 AA.
AC A0A1V8SSF5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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=B0A48_11669 {ECO:0000313|EMBL:OQO02117.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO02117.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:OQO02117.1}.
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DR EMBL; NAJO01000028; OQO02117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8SSF5; -.
DR STRING; 1507870.A0A1V8SSF5; -.
DR InParanoid; A0A1V8SSF5; -.
DR OrthoDB; 1332545at2759; -.
DR Proteomes; UP000192596; 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:UP000192596};
KW Transferase {ECO:0000256|RuleBase:RU367084}.
FT DOMAIN 170..561
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 86966 MW; 534041244ACB10C1 CRC64;
MPRSRPQGGT SGYERIVQAE EAEEEDPHNY DHDEGPFQDP LRLSTSDDTH FSPIQPKRRE
RMHIPSGSNS PRRSGRRRRT NSGVDIKAIN ARLERWADEI KDKFTIRKVR GKSAQDEHLE
IYQSVFQAPE GVRPATKELL EADHAEPGEK LSKLEFDEMV ESVRTAIELG LHPTLIAQGS
SGSYFARNSS GRVLGVFKPK DEEPYASKNP KWTKWIHRNL FPFGFGRACL IPNLSYVSEA
AAYVLDCQLR TNLVPYTEVV SLSSKSFFYD YWDRRQHYRK GKPLPEKQGS FQVFLKGYKG
ATEFFQEHPW PDHHNGGFRD APKRTKRRRW AEDCRPASVV GDVSDAEDDG PTGAQSRARL
EFWTDALRES FREQLEKLVI LDYIMRNTDR GTDNWMIKVD EQKQTAEVVL EPPKDDSMLN
GNADPYHRRQ ESMSTTPGGD GPTAVPSIGA IDNSLSWPWK HPDAWRSYPF GWLFLPVSLI
GRPFSAKTRA HFLPLLTSKD WWSDTQVKLR QCFEIDADFK ERMFARQIAV MKGQAWNVVE
TLKTPDHGPL ELTRRDRACV WDDLVEVPVA VHMSRPSEEM RRSAHRLRAE QAREIRQVHS
SSEQGEMDIS AAMGSAPQPN HDLLGFNSSP VREFAQNPFN YSRHNSSEIV PQSEDSTEPL
STTAPITFDL PPTPSRKRPT TTRAHTGDNC TSQEASRRHW QPQSERRRRF SLGRRSSGLS
EGSDGDGDLG FVAAREQEGS RRKVIVERLE MIKGKPPVFS WC
//
