ID A0A366SAZ0_9HYPO Unreviewed; 916 AA.
AC A0A366SAZ0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-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=FIESC28_00687 {ECO:0000313|EMBL:RBR26501.1};
OS Fusarium coffeatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR26501.1, ECO:0000313|Proteomes:UP000253153};
RN [1] {ECO:0000313|EMBL:RBR26501.1, ECO:0000313|Proteomes:UP000253153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR26501.1,
RC ECO:0000313|Proteomes:UP000253153};
RA Gardiner D.M.;
RT "Fusarium incarnatum-equiseti species complex species 28.";
RL Submitted (JUN-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:RBR26501.1}.
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DR EMBL; QKXC01000019; RBR26501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366SAZ0; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000253153; 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; 1.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 18..195
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 365..551
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 632..900
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 239..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 103977 MW; 52EF9909642FD8D0 CRC64;
MSEYGRMDPF SFAGSKDVHH PVSIRIMNLE GEEPPFRSST LLERPDLRHI GSNISPYSDL
YVTVQVWSGS KPLTVPVQTA YKPFRFERKW NEWIQLPITY DSLPANSCLA ITVWDLSPVG
GDGAIGHAIP FGGTTLAMFD DDNQAQKGRQ KCLVHRHKHA DGTDNTTTPA LISTKKKTSR
KEQLPPLDKD AEELDRMETL FKKHEMGEIP RVDWLDQMVF RSFEKRGLQA AKSSMKMLQR
QQAISGEHET DGQDGEDNHE RPGQSTFLLN VELPRFDFPV VFADHEYGPP PISALQNLSV
SQASLAHRQP QVQYGPGINA LGESSAALGG RLIKVYDPEA GHRDNPAEAK HRRLFRSSHR
HGILDKDLKP NAKVRDELNL IMSYSPTHVL TPEETDLVWK FRYHLTRDKR ALTKFVKSVN
WNDQSESRQA IQVLGRWTAI DVDDALELLG PSFDNSAVRS YAVERLRKAD DEELLLYLLQ
LVQALKYEHI STESDEESIH DSSLARFLIQ RAAANFLLGN YFHWYLMVEC DDPSPEQGVD
NRNIYRKVAY DFMVELVKQP DGQETRKILL RQAELVAILS KIAQEVKTSN ESIAKKVDKV
KHFLADPKNE LLTFEPPLPM PLDPSVLVTG IIPDQTVVFK SSLNPFKCTF KTSTGSPYPI
IFKLGDDLRQ DQLVIQIITL MDQLLQKENL DLKLSPYKIL ATSTSAGASQ FVQSASLSSI
VNKFKNNPAL AYLKYHNPDD RQPLGVRQET LDTYVRSCAG YCVITYILGV GDRHLENLLL
APDGHFFHAD FGFILGRDPK PFAPLMKLSK EMVDCMGGVQ SEHYKQFKQY CFLAYTALRK
SSNLILNLFS LMVDANIPDI RLEPDKAVLK VRERFHLELS EEEALRYFDR VIEDTLTAYA
PVVIDKLHEW AQAFRT
//
