VPS34_CANAX
ID VPS34_CANAX Reviewed; 1020 AA.
AC Q92213;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phosphatidylinositol 3-kinase VPS34;
DE Short=PI3-kinase VPS34;
DE Short=PI3K VPS34;
DE Short=PtdIns-3-kinase VPS34;
DE EC=2.7.1.137;
DE AltName: Full=Vacuolar protein sorting-associated protein 34;
GN Name=VPS34;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3153A;
RX PubMed=10870104;
RX DOI=10.1002/1097-0061(200007)16:10<933::aid-yea591>3.0.co;2-c;
RA Eck R., Bruckmann A., Wetzker R., Kunkel W.;
RT "A phosphatidylinositol 3-kinase of Candida albicans: molecular cloning and
RT characterization.";
RL Yeast 16:933-944(2000).
CC -!- FUNCTION: Phosphatidylinositol 3-kinase homolog required for vacuolar
CC sorting and segregation.
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;
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00880}.
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DR EMBL; Y09043; CAA70254.1; -; Genomic_DNA.
DR PIR; T18260; T18260.
DR AlphaFoldDB; Q92213; -.
DR SMR; Q92213; -.
DR VEuPathDB; FungiDB:C1_06680W_A; -.
DR VEuPathDB; FungiDB:CAWG_00745; -.
DR BRENDA; 2.7.1.137; 1096.
DR PHI-base; PHI:195; -.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR Gene3D; 2.60.40.150; -; 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; PTHR10048; 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; SSF48371; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..1020
FT /note="Phosphatidylinositol 3-kinase VPS34"
FT /id="PRO_0000088816"
FT DOMAIN 49..210
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 331..577
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 666..1004
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 672..678
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 873..881
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 892..913
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 1020 AA; 117401 MW; FF798F55AD2C8231 CRC64;
MATLSQPQSA LPKTKIATTF GLSKDLKSPI SVKVCYLECT RNNVSLVPLS TKFEDPTVFK
KLSQIYKNSD LFVEIRVYDG KNNNLISTPV RTSYKAFNNK GRTWNQQLKL NIDYNQISID
AYLKFSICEI IDTKPSVFGV SYLSLFSHDS STLRSGSHKI PVFMEDDPQY SKNIQYGTLI
GLTDLEKRLI DYENGKYPRL NWLDKMVLPK VDATFLKTNN KDHDYYLYIE LPQFEFPIVY
SDIIYQIPTI EPITETTSKI PPDDTLNSNI IINSIDIPMA TSHDPSIMKV YDPDFHITAN
NHLNPNATTF DPVELKYRKL ERNIDNNTIL DKELKPTPQL RDELLRIMIK PSNAESTDNE
KNLIWKFRYY FSKNNSGNDP SNKSVKSFLP KFLRSINWEN DYELDHTFKE IIPFYWNVDK
LQIGDALELL GDYFNPYTLG KPTYQDDSMT SKSSKMKSDE KRFIKIYNNV CFLRKLAVER
LKLANSEELL LYLLQLVQAL KYEALIYEKS PPFCERSDQI EDNASSTLKS PLADFLIERA
VENEKLGNFF YWYVKVENED QLNNPHIDGP IKIYMDILNR YIELLKAHCH ENRLPYYKHL
KHQIWFIKKL TSLVELLRAS FKKNEATAKK VEYLREYLAN SGNELLKFPE PFPLPLDPSV
MICGCYPEES SVFKSSLAPL KITLKTIEKK KHGHATSQLF GKRSRYGKYP LMFKIGDDLR
QDQLVIQIID LMDQLLKNEN LDLKLTPYKI LATSPISGLI QFVPNETLDS ILSKTYPTSV
TYSGGGETSD GPPSVSNNGI LNYLRLHSQE QQSEEPISKS ILSTNTSQSN TEIPVLPRQP
KPTITSDLGV SPILMDNYVK SCAGYCVITY ILGVGDRHLD NLLLSPNGKF WHADFGYILG
RDPKPFPPLM KLPIQVIDGM GGLHHENYNV FKSYCFITYT TLRKNSNLIL NLFQLMLDAN
IPDIQFDPSR VIEKVQEKFC LQMTEEEAIL HFQNLINDSV NAFLPVVIDR LHSLAQYWRA
