(data stored in SCRATCH zone)

SWISSPROT: Q750Q5_ASHGO

ID   Q750Q5_ASHGO            Unreviewed;       870 AA.
AC   Q750Q5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 136.
DE   RecName: Full=Phosphatidylinositol 3-kinase VPS34 {ECO:0000256|PIRNR:PIRNR000587};
DE            EC=2.7.1.137 {ECO:0000256|PIRNR:PIRNR000587};
GN   ORFNames=AGOS_AGL113C {ECO:0000313|EMBL:AAS54378.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54378.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54378.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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|PIRNR:PIRNR000587};
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC       {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE-ProRule:PRU00880,
CC       ECO:0000256|SAAS:SAAS01097356}.
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DR   EMBL; AE016820; AAS54378.1; -; Genomic_DNA.
DR   RefSeq; NP_986554.1; NM_211616.1.
DR   STRING; 33169.AAS54378; -.
DR   EnsemblFungi; AAS54378; AAS54378; AGOS_AGL113C.
DR   GeneID; 4622853; -.
DR   KEGG; ago:AGOS_AGL113C; -.
DR   HOGENOM; HOG000174003; -.
DR   InParanoid; Q750Q5; -.
DR   KO; K00914; -.
DR   OMA; LHKFAQY; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0071561; C:nucleus-vacuole junction; IEA:EnsemblFungi.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IBA:GO_Central.
DR   GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IBA:GO_Central.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0046854; P:phosphatidylinositol phosphorylation; IBA:GO_Central.
DR   GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IEA:EnsemblFungi.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:2001159; P:regulation of protein localization by the Cvt pathway; IEA:EnsemblFungi.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   Gene3D; 1.25.40.70; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
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; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR002420; PI3K_C2_dom.
DR   InterPro; IPR008290; PI3K_Vps34.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048; PTHR10048; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 2.
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; SSF48371; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; PS51547; PI3K_C2; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750Q5.
DR   SWISS-2DPAGE; Q750Q5.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000587};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE-
KW   ProRule:PRU00269, ECO:0000256|SAAS:SAAS00936663};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE-
KW   ProRule:PRU00269, ECO:0000256|SAAS:SAAS00936588}.
FT   DOMAIN          27..185
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          291..521
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          614..868
FT                   /note="PI3K/PI4K"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   870 AA;  99322 MW;  95821FD1894CA5CE CRC64;
     MPSQSVTFVV SQELNIPLKI KISSLHGTKK LLQPSQRFTH PELTQRTSNM RLNSDMFVSV
     QVFDRERNRA LTTPVHTQYV PFKTGRVWNQ WLTLPIYINQ LDRNSTLQIT IWEYDAANCI
     EFATLKTPVF SDADCTLKRG REALHFEYGA PESSRVEGDA IQGLLNKYDQ GGIKAIDWLD
     SLTFKKLESM QREADLPKGT FRLNIEFPLF ELPVVYTEAT NTNVQKNIPT LNNFEPPSET
     IESKMDSQAK ISVGSPRQST LKFYDLDQYN VDVIEEKFRR LERSSKSSNL DRELKPDAKK
     RDILNHIIAY PPCTSLTPHE KGLVWKYRYY LVNNKKALTK LLQSTNLAEE NERKEVLDLM
     DLWAEIDIDD AIELLGPVYK NLSVRSYAVN RLKKASDTEL ELYLLQLVQA VCFESSSTWS
     DKSNSAFTIV HMDQSKNGNC TPKSLTPHMT ASLDSLDRSD VESNGAESSI VISPLAEFLI
     RRVVNNTRLS NYFYWFLKSE SKGTQYLVHI LDSFLVRLSQ ESRGQIEDQV QLVNLLKECC
     CEVKQLKDTT PKKHELLHYL MLSKVRPFLR ATNVALPLDP EVVAVDVVPE DCKVFKSSLS
     PLKITFKTKD ARKYSLMFKV GDDLRQDQFV VQIITLMNAL LKNENVDLKL TPYRILATGH
     NEGAIEFIPN DTMANILSKH HGILPFLKSN FPDRGEPLGV QDWVMDNFVK SCAGYCVITY
     ILGVGDRHLD NLLIAPDGRF FHADFGYILG RDPKPFPPLM KLPPQIIEAF GGAESNNYNK
     FRSYCFVAYS ILRRNAGLIL NLFELMKTSD IPDIQMDPDG AILKVKEKFC LNMSEEQATV
     HFQNLINASV NALLPLVIDH LHNLAQYWRS
//

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