ID A0A1G4IXV9_9SACH Unreviewed; 866 AA.
AC A0A1G4IXV9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=LADA_0C00848G {ECO:0000313|EMBL:SCU81746.1};
OS Lachancea dasiensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU81746.1, ECO:0000313|Proteomes:UP000190274};
RN [1] {ECO:0000313|Proteomes:UP000190274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-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-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; LT598459; SCU81746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4IXV9; -.
DR STRING; 1266660.A0A1G4IXV9; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000190274; Chromosome C.
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:UP000190274};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 32..185
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 289..517
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 584..850
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 866 AA; 98857 MW; 0376B72D156AD61D CRC64;
MSVKSVTFCI SNELGLPLQV KIDSLEGSKP LLKTSQRLTK PSLSQRTSDV LANSDMFVSV
QVFDKESQRN LTIPVYTPYI PFKSSRKWDV WLTLPITLEQ LTAHSMLSII LWEFDGDNEV
EFFSVETPLF EERSRSLKRG TEAIRFQIDD PDSGRIETNE VQDLVNKYKQ SEIKAVDWLD
GITLPQLEKS LRKRKLPPGT FVLNIEYPLF ELPIVYSEKI SDKALKNVPN FHNFDVINDQ
VARQDSQAKL SLGSGTESTL KFYDPDQFNV DPIEEKFRRL ERATTNSSFE KELKPDLKKR
DVLNQIISYP PGSDLTAHEK GLVWKYRYYL MNNKKALTKL LQSTNLTEEN ERKEVLELVD
SWAEIDIEDA IELLRSAYKN LSLRSYAVNR LKKASDNELE LYLLQLVQAV CFESASPLSD
KSASEFTIVD VMQSTAPVPA SPKYDHSNGA NSINSVESTA MGQSSVLISP LAEFLIRRAI
INDRLGNFFY WYLKSESEGN QYLIYILDSF VSRLPNNKRA KLDNQIEFMS MLENFCQEIK
NLRDTTPKKL ELLLHLISTK MKPFLKSKPV ELPLDPDYVL TDVVSGGCKI FKSSLSPIKI
VFTTQGQENY SLMFKVGDDL RQDQLVVQII SLMNELLKNE NVDLKLTPYK ILATGSREGA
IQFIPNDTMA SILNKHHGIL PFFRTHHPSP DNELGVQEWV MDNFVKSCAG YCVITYILGV
GDRHLDNLLI TPDGHFFHAD FGYILGQDPK PFPPLMKLPP QIIESFGGAE SQNYDKFRSY
CFVAYSILRR NANLILNLFE LMKPSEIPDI KIDPDGAILK VKEKFCLDMS EEEAIIHFQN
LINASVNALL PLVIDRLHNL AQYWRA
//
