ID A0A1E3I3G8_9TREE Unreviewed; 895 AA.
AC A0A1E3I3G8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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=L202_01335 {ECO:0000313|EMBL:ODN83132.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN83132.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN83132.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN83132.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-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}.
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:ODN83132.1}.
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DR EMBL; AWGJ01000002; ODN83132.1; -; Genomic_DNA.
DR RefSeq; XP_018997132.1; XM_019134705.1.
DR AlphaFoldDB; A0A1E3I3G8; -.
DR STRING; 1295533.A0A1E3I3G8; -.
DR GeneID; 30152644; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000094065; 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; 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:UP000094065};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 34..187
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 300..504
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 581..881
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 895 AA; 101901 MW; F1F460FDE9147CE7 CRC64;
METEPSRDRD YSFARLCDIK SPVTLKITSL EGKLPQSSHI EALNHAGVIR SKANTPIPDL
YITCMLWTGE AQHTLPFRTG WKDLSRGTKW NQTIILPVQY PSLLLESSVT FTIWDVQESG
RCTAIGGTKM ALFDHHRTLK RGQQRLYIHR GVEADPRPNS TTPSEVLNRE DDEMGRLESL
IKEFDRGDIN KVEWLDRLAF RKLEKAHLRE ASKSKDMYLY VDLPKFDFPV VYSEQESLLS
VPPAPVAHLF PTIPPVLALP PNFLSSDRHL WRAYDPDAWR DNPVEIKHRK LLRSQRLGDA
GKDLKPGPSD RDRLNDIFRL PPTASLSAFD KDLLWKFRFS LFRSPRSLTK FLKCVTWSDP
VETKQAVEKL LPLWGQDVGI DDALELLGPE FMHKKVRAFA VKRLERADDE ELLLYLLQLV
QALKFEHKYF LSSQRPHKPR AHQLKRQLSQ DEASDSGLSQ FLIDRSVSNP ILSTRFHWYL
MIECDSRVPA GRMYAKIAHD FMNKLSQSPE GTAQREVLRR QGVLVQTLST RAREVRLSKD
PRQKKIEKLK AYLSDPKNGL SSFAEPLTLP LNARVSVTSV VAEKSSIFKS NLLPLLIWFE
TAEPNRAAED DSEGIVNISP DYPVIFKNGD DLRQDQLVIQ LFTLMDRLLR KENLDLRLSP
YSVLATSTSE GLIQFVPSKS VASIMAEHGN LQNYLKLEHS DDAALGSYGI EAGVMDTFVR
SCAGYSVLTY VLGVGDRHLD NLMLAPDGHF FHGTSWGNHS IRDMLRPSVV DFGYILGRDP
KPYPPPVKVC KEMVDAMGGT GSAHYSRFQS LCYTAFTGLR KNANLILNLV ALMVDAGIQD
IQLEPDKAVW KVQEKFMLDL SEEDAIKQFE VLLNDTSYLT VVFDRIHDWA QYLRD
//
