ID A0A067M565_9AGAM Unreviewed; 849 AA.
AC A0A067M565;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=BOTBODRAFT_167791 {ECO:0000313|EMBL:KDQ06726.1};
OS Botryobasidium botryosum FD-172 SS1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Botryobasidiaceae; Botryobasidium.
OX NCBI_TaxID=930990 {ECO:0000313|EMBL:KDQ06726.1, ECO:0000313|Proteomes:UP000027195};
RN [1] {ECO:0000313|Proteomes:UP000027195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-172 SS1 {ECO:0000313|Proteomes:UP000027195};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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}.
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DR EMBL; KL198125; KDQ06726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067M565; -.
DR STRING; 930990.A0A067M565; -.
DR HOGENOM; CLU_004869_0_0_1; -.
DR InParanoid; A0A067M565; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000027195; Unassembled WGS sequence.
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: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; 1.
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:UP000027195};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 19..186
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 299..493
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 569..835
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 849 AA; 96723 MW; DD3FEB36C952FE7B CRC64;
MDAGKDTTKD VTFAKLSDLK FPVTVRISQL EGTRKPRDFS ELIVHPELRF AGVQSETLSD
LYVTCQILAD NKPLTIPYRT CFKAFKNNYT WNEWITFPIK YCDLPLNSQI TFTVWDIAGP
RSAVPVGGST FKMFGKKWTL RRGKHRLLLW PEQEADGSVE SRTPSKVGLK DEMGRLEKLV
KKFERGDLPK QDWLDKLAFR RMEETHAAET EKSNSLFLYI DLPRFDFPVI FSEPESAPTP
ATSVVVPNPP PGGPITSALI NFNTDPNLWA VLDPEIAREN PVEDKHRRLV RSHRTGPLDR
ELKPNADIRD ELSEILNYAP TQLLTSEEKD LIWQFRFYLT RDKRGLTKFI KSVTWRDATE
VKQAVEVLLP MWTDIEMDDA LELLGPGTVD SRVRAFAVRQ LARADDDELL LYLLQLVQAL
KFENTASGRT MRSTSRSGIS YDDSGLADFL IDRGARNPVL GNRFYWYLMV EMEDKDKTLG
ELYKRLTWSF MNKIIQMENG ADRRDILRRQ GELVATLSAR AKELRASKDS RPKKIDKLRA
FIADPKNNLM SMSPLPLPLN ARVEITGLVA EKCSVFKSNL SPLLIYFQCS DGGEYPIIFK
NGDDMRQDQL VIQLFTLMDR LLRKEMLDLK LTPYNVLATS TLEGMAQFIP SKTIAAIVSE
HATLLNYLRA HNPDEGSVGT YGVTPSVIDT FVRSCAGYCV VTYILGVGDR HLDNLLLTPD
GHFFHVDFGY ILGRDPKPFP PLVKVCKEMV DGMGGAGSSH YARFKNLCFT AFTILRKSAN
LIFNLMSLMV DANIPDIQHG NVHEQIRDKF QLDLTEEEAI KHFETLLNET SYFTVVLDRI
HDLAQYWRS
//
