ID A0A094D4S4_9PEZI Unreviewed; 949 AA.
AC A0A094D4S4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Phosphatidylinositol 3-kinase VPS34 {ECO:0000256|ARBA:ARBA00041128};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
DE Flags: Fragment;
GN ORFNames=V496_05021 {ECO:0000313|EMBL:KFY61406.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY61406.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY61406.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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:KFY61406.1}.
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DR EMBL; JPJY01000864; KFY61406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094D4S4; -.
DR STRING; 1420909.A0A094D4S4; -.
DR HOGENOM; CLU_004869_0_0_1; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000029302; Unassembled WGS sequence.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08397; C2_PI3K_class_III; 1.
DR CDD; cd00870; PI3Ka_III; 1.
DR CDD; cd00896; PI3Kc_III; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR008290; PI3K_Vps34.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 3.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000029302};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..199
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 356..542
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 624..895
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 150..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 949
FT /evidence="ECO:0000313|EMBL:KFY61406.1"
SQ SEQUENCE 949 AA; 106326 MW; BBDE7E5CB40ADE56 CRC64;
MDPFSFASSE ALELPLNVKI VRLEGEQTQI PFSTLIKRPD LRHIGSNISP HSDLYLTVQL
WADSKPLTVP VRTPYKPFKN ERKWGNWLTL PVTFNTLPLT AQLAITVWDV SPAGGDGAQG
HSIPFGGTTF PLFDKENTLQ KGRQLCHLHR RKAADGLAGT STPASLPTRR SEKNGKPENG
LVDKEQEEAE RLEKLLKKHE MGEIPRVDWL DQLVFRNIEK QNILSSSPSA KSLQNRRSKP
DGEITTLDGE VEADIENEVF TLHIELPRFD FPVVFSDHEY PPPPISSMQH LSTSQNNILK
PPPAVYFGPG VDGEPDDGSF GGRLVRIYDP EVGSRDNPAE TKHRRLVRGH RTGAMDRDLR
PNARFRDELN QIVGSPPTHA LSPDEKDLIW KFRHHLTKDK RALTKFVKSV NWQDNSEARQ
AVQLLSKWTE IDVDDALELL GPSFDNSDVR AYAVDRLRKS DDDELLLYLL QLVQALKFEH
KTPNSSDEPK ADSSLAQFLI ARAAKSFMLG NYFHWYLMVE CDDKSAGQPP QYRKLFAKVE
YDFMIELEKT PTGKETRKTL LRQAEFIAVI SKISLETSAK GGPTIAKKTE RAKQFLVDPK
NELNNIDPPL PLPLDPSILI SGVYPEETSV FKSSLSPLKM TFRTSSGRHY PIIFKTGDDL
RQDQLVIQII TLMDQLLRKE NLDLKLSPYK ILATGATAGA VQFVPSSSLA AISTKHRSSG
HPPILTYLRT HNPDSSAPLG VRKEAMDTYV KSCAGYCVIT YLLGVGDRHL DNLLLAPSGH
FFHADFGYIL GRDPKPFAPL MKLGSEMADG MGGQQDENWA RFKEYAFTAY AALRKQSGLV
LNLFGLMVDA NIPDIRAEPE RVVEKVMERF MLEMSEEEAI RGFERIIEDS VGAIFPVARS
EVQEAREERV MLSWGRGHVA GDEDGDDEGV DGDDAGHDDR DEGLDWGVG
//
