ID A0A2P7YHP2_9ASCO Unreviewed; 1018 AA.
AC A0A2P7YHP2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=C7M61_004516 {ECO:0000313|EMBL:PSK35479.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK35479.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK35479.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK35479.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) 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:PSK35479.1}.
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DR EMBL; PYFQ01000015; PSK35479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YHP2; -.
DR STRING; 418784.A0A2P7YHP2; -.
DR EnsemblFungi; C7M61_004516_t1; PSK35479.1; C7M61_004516.
DR VEuPathDB; FungiDB:C7M61_004516; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000241107; 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: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; cd00896; PI3Kc_III; 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; 2.
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:UP000241107};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 55..209
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 345..580
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 674..1002
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 303..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 115434 MW; D9B55189DD80233C CRC64;
MSQGGAQTVE ASDAGLLLLL STNTATFGLS KHLLIPLFVK IRSLETTHKF KPASSSAKYK
NPDLFQVLSK ILASSDLFVK VEVLDGNNNR IIPPVQTPYR QFLGNKRIWD AVMKLPILYS
QLDYSAYLRF ELFEIVQTKP VHFAEGRLSL FNHENGSLRK GTYKVPISQD SAAVNYKTEF
CTTPLEDRMI NYENGALKKE PWLDSLLLPI AEKLKHQETC PGDAPYHLFV ELPNFSLPIV
FLDITYELPT MEMLPQADFD KTQLGTENAG AMVLTSVDLT PRKLYDPDFD FLTLHNFNTT
GEASVSGSAG VPGQSGGSLT RRAPLDPIEK KFNILSTSVN NNSLLDKEVK PSPQDRDELG
KILRKPLSAI LADHEKRMLW KYRYYFSKNL GDESQISGPL QSQRQFLTKF FKCFNWENEQ
ELDHAMKEIL PYWSVEKIDM GDALELLSNQ FNPHNLTAAL RRRLVDTSGA SRDINTAEEQ
KIEKIFKSAM KLREFAVDRL KLASADELLL YLLQLVQALK YEVIEENPNL DKAPLAKFLL
QRSVENGILG NFFYWYVKVE NEDQLNGGEV VPQSKAVNGA IYGVVLNTYI EKLRTFCQKT
KLPQYKYLKR QIAFIKKLTS LVEKIRTTFK RNEATAKKVQ FLREYLADPL NEMLLFPDPF
PLPLDPSVII CGCHPEESSV FKSSLAPLKI TFKTITNFKE RLSSSHSSQI FGGTKKHKYG
KYLLMFKIGD DLRQDQLVIQ IINLMDQLLK NENLDLKLTP YKILATSPVA GLIQFVPNET
LDAVLSATYD NVGPSQSATT ANGILRYLQL HSRMLHHEEP ESQSVLGKKK NSIPLQDQEH
AVSSDLGISP TLMDNYVKSC AGYCVITYLL GVGDRHLDNL LLSPNGKFWH ADFGYILGRD
PKPFPPLMKL PIQVVDGMGG MTHENFNIFK NYCFITYTTL RRNSNLILNL FQLMLNANIP
DIQIDPKRVV EKVEEKFALE MTEELAILHF QNLIIDSVNA FLPVVIDALH SLAQYWRA
//
