ID A0A0A2V871_BEABA Unreviewed; 903 AA.
AC A0A0A2V871;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Phosphatidylinositol 3-kinase VPS34 {ECO:0000256|ARBA:ARBA00041128, ECO:0000256|PIRNR:PIRNR000587};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073, ECO:0000256|PIRNR:PIRNR000587};
GN ORFNames=BBAD15_g12244 {ECO:0000313|EMBL:KGQ02547.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ02547.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ02547.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ02547.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ02547.1}.
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DR EMBL; ANFO01001476; KGQ02547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2V871; -.
DR STRING; 1245745.A0A0A2V871; -.
DR eggNOG; KOG0906; Eukaryota.
DR HOGENOM; CLU_004869_0_0_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:EnsemblFungi.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0071561; C:nucleus-vacuole junction; IEA:EnsemblFungi.
DR GO; GO:0005777; C:peroxisome; IEA:EnsemblFungi.
DR GO; GO:0000407; C:phagophore assembly site; IEA:EnsemblFungi.
DR GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IEA:EnsemblFungi.
DR GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IEA:EnsemblFungi.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:EnsemblFungi.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IEA:EnsemblFungi.
DR GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
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 ATP-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000587};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 19..183
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 352..542
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 619..887
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 903 AA; 102094 MW; 4044999EC68BD4B9 CRC64;
MTLITPSASE CKSDDAAALE KRETNTLHRS DLRHVGSNMS VYSDLFVTSQ VWAGSKALTV
PVQTAYKPFR AERRWNEWLQ LPISYRSLPS DSCIAITIWD LSPNGGKDSQ GNAIPFGGTT
LPMFDAENQT RKGRQKCLLH RHKMADGTAR METPAILTSR KKALTGEVGI QAARDAEELK
RMESLFKKHE MGDIPKIDWL DQLVFRDFEN RGLKAAESSL KMLQRRRRLV SRKSESPDDV
ADQTIDYSSP PAFILNVELP RFDFPVVFGD HEYHVLPISA LATVHFHQPG QHRQQAPEVQ
FGPGINAVDD SLSAIGARIA KVYDPEVGQR DNPAETKHRR LFRSSHRHGI LDKDLKPNAK
VRDELNTIMN YSPTHTLSPE EMDLVWKFRY HLTRDKRALT KFAKSVNWND QSESKQAIQV
LGRWTEIDVD DALELLGSSF SSPGVRSYAV DRLRKADDHE LLLYLLQLVQ ALKYEHISTE
TVEGALEDSS LARFLIQRAA SNFLLGNYFY WYLMVECDDN SPEQGAHSRD IYNKVAYDFM
RSLTKQPNGD DERKTLLRQA ELVSVLSKIA IDVRKSGESM SKRADKVKTL FADPSNELIV
IDPPLPLPLD PSIKITGILP DQVTVFKSSL SPIKCSFKTI DGDSYPIIFK VGDDLRQDQL
VIQIITLMDQ LLQKENLDLK LLPYKILATS TAAGASQFVQ SQSLSSIVGK YKNNPALAYL
RYHNPDNMQP LGVRQEALDT YIRSCAGYCV ITYILGVGDR HLDNLLLAPD GHFFHADFGY
ILGRDPKPFA PLMKLSKEMV DCMGGVQSEY YKQFRQYCFL AYAALRKSSN LILNLFSLMI
DANIPDIRLE PDKAVIKVRE RFHLELNEEE AMVSLGRVID DALASYAPVV IDKLHEWAQA
LRS
//
