ID R1GF31_BOTPV Unreviewed; 869 AA.
AC R1GF31;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=UCRNP2_6385 {ECO:0000313|EMBL:EOD46871.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD46871.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(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|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}.
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DR EMBL; KB916378; EOD46871.1; -; Genomic_DNA.
DR RefSeq; XP_007585650.1; XM_007585588.1.
DR AlphaFoldDB; R1GF31; -.
DR STRING; 1287680.R1GF31; -.
DR KEGG; npa:UCRNP2_6385; -.
DR eggNOG; KOG0906; Eukaryota.
DR HOGENOM; CLU_004869_0_0_1; -.
DR OMA; LHKFAQY; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000013521; 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 Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 12..178
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 317..503
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 584..853
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 187..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 98896 MW; B553A099A071BB8C CRC64;
MEPFSFASSS ALDLPVHVRI NNLDGHQKPI PFSTLPHSEL FVTAQLWADS KPLTVPVQTS
YKSFKSTRLW NEWLTLPVSY ATIPQSSQLA ITVWDLSPTE DSQIHATPFG GTTIPLFDKE
NTLQKGRQRC RIHLSRAADA EEVDPDMTEM ERLEALMKKH EMGEIPENRW LDQMVFRKME
QLERNTYRSG PKYARKTDAP KSNGIEDDDG SEDESLDEDK FFLYVEFPRF DHPIVFTDRE
YPAPPISTMQ SSSLSDIRLK PPPEVSFGPG INDGVGEDDP EIGRMIRIYD PEVGIRDNPA
ESKHRRLVRN HRTGVMDRDM KPNAKARDEL NVIMSYGPTH ELSADDKDMV WKFRHHLTRD
KRALTKFVKS VSWSEPGEAR QAVQLLSKWT EIDVDDALEL LGPTFDHPAV RSYAVDRLRK
SDDDELQMYL LQLVQALKFE PVQTDSDGEP TQDSSLARFL INRAAGNLNL GTFFHWYLMV
ECDDRSPEQG SEHRKLFAKV EYDFMTTLME TEDGPARRKV LLRQGELITV LSKISKEIRF
SRDDRLRKIE SLKQFQADPK NELIHIDPPL PLPLDPTVEV VGVFPEDCNV FKSSLFPLLI
NFKTATGAKY PVIFKTGDDL RQDQLVIQII TLMDRLLRLE NLDLKLSPYR ILATSTTAGA
VQFVPSTPLA SAVTKYKGQG SILSYLRANN PDESAPLGVR KEAMDTYVKS CAGYCVITYL
LGVGDRHLDN LLLAPDGHFF HADFGYILGR DPKPFAPLMK LDNLMIAGMG GPNSPNFTAF
KNYCFTAYTT LRKQSSLILN LFSLMRDANI PDIKIERDKA VWKVQERMCL DMTEEEAIRH
FEGLIQDSLN AVMPLVIDRL HGLVQNWRA
//
