ID A0A1J9QN76_9EURO Unreviewed; 912 AA.
AC A0A1J9QN76;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=AJ78_03163 {ECO:0000313|EMBL:OJD16693.1};
OS Emergomyces pasteurianus Ep9510.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD16693.1, ECO:0000313|Proteomes:UP000182235};
RN [1] {ECO:0000313|EMBL:OJD16693.1, ECO:0000313|Proteomes:UP000182235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD16693.1,
RC ECO:0000313|Proteomes:UP000182235};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA McEwen J.G.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) 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:OJD16693.1}.
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DR EMBL; LGRN01000096; OJD16693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9QN76; -.
DR STRING; 1447872.A0A1J9QN76; -.
DR VEuPathDB; FungiDB:AJ78_03163; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000182235; 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; 2.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 3.
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:UP000182235};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 28..197
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 364..550
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 629..896
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 156..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 103259 MW; 18E026EE17E9D455 CRC64;
MDTYTFATSA QVDLLIQVKI CSLEGKQKPI PFSVLIKNPE LRHLGSNQSP ISDLYVTVQL
WAGSKPLGVS AQTAYKAFRT SRTWNEWLTM PVSIKDAPIN TQLAITVWDL SPLGGNDAYG
HSVPFGGTTI SLFDDDGTLK KGRQKCKIYR HKAADGLSNT TTPSTPAQKR RLSPHINHGP
TPEEEELERL EKLLKKHEMG EIPRVDWLDQ LVFRAVEKKK LDAEESAKKR AIRNQASRAK
VATKANGETD NLDDVEEDDG VNDHEENFVL YVEFPRFDFP VVFEDFEYPR PPISSHSQQP
LSGSNSTLKP PPEVRLGPDI DGAGNEDDDH RIIRIYDPEV GQKGNPCEDK HRRLVRSHRT
GIMDRDLKPN PKIRDELNDI MLYGPTQELN AEEKDLVWKF RHHLTRDKRA LTKFVKSVNW
QDVGEARQAV EILPKWTEID VDDALELLGP TFDNPAVRAY AVDRLRKSDD EELLLYLLQL
VQALKFEAIP DEATEHGTED SSLTNFLITR AASNPLLGSY FHWYLMVECD DAGPSTISAH
RKLFARVEYY FMVELEKHHP EQRKILLRQG ELITILSKIA KDIRFSRVNR AVKIEKLKKF
LLDPKNELAT IDPPLPLPLD PEILITGCFA EGSNVFKSSL SPLLINFKLS DGRKYPVIFK
VGDDLRQDQL VIQIISLMDR LLQKENLDLK LTPYRIIATS ANAGAMQFIP STSLSAASAK
YKGSILAYLR ANNPDDNEPF GVRKETMDTY IKSCAGYCVI TYLLGVGDRH LDNLLIAPDG
HFFHADFGFI LGRDPKPFAP MMKLCKEMVE GMGGASSPNY LLFKQYCFTA YTTLRKSANL
ILNLFSLMVD ANIPDIRVEP DKAVLKVKER FHLEMTEEEA IRHFEQLIGD SVNAIFGVVI
DRLHDFVQGW RA
//
