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Database: UniProt
Entry: A0A8X7V556_BRACI
LinkDB: A0A8X7V556_BRACI
Original site: A0A8X7V556_BRACI 
ID   A0A8X7V556_BRACI        Unreviewed;       813 AA.
AC   A0A8X7V556;
DT   14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 1.
DT   28-JAN-2026, entry version 13.
DE   RecName: Full=phosphatidylinositol 3-kinase {ECO:0000256|ARBA:ARBA00012073};
DE            EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
GN   ORFNames=Bca52824_031218 {ECO:0000313|EMBL:KAG2302567.1};
OS   Brassica carinata (Ethiopian mustard) (Abyssinian cabbage).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=52824 {ECO:0000313|EMBL:KAG2302567.1, ECO:0000313|Proteomes:UP000886595};
RN   [1] {ECO:0000313|EMBL:KAG2302567.1, ECO:0000313|Proteomes:UP000886595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sxm20200214 {ECO:0000313|EMBL:KAG2302567.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAG2302567.1};
RA   Ma Q., Huang Y., Song X., Pei D.;
RL   Submitted (FEB-2020) 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:ARBA00001498};
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC       {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE-ProRule:PRU00880}.
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:KAG2302567.1}.
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DR   EMBL; JAAMPC010000007; KAG2302567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8X7V556; -.
DR   OrthoDB; 67688at2759; -.
DR   Proteomes; UP000886595; Unassembled WGS sequence.
DR   GO; GO:0005768; C:endosome; IEA:TreeGrafter.
DR   GO; GO:0005777; C:peroxisome; IEA:TreeGrafter.
DR   GO; GO:0000407; C:phagophore assembly site; IEA:TreeGrafter.
DR   GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IEA:TreeGrafter.
DR   GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IEA:TreeGrafter.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:TreeGrafter.
DR   GO; GO:0006897; P:endocytosis; IEA:TreeGrafter.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:TreeGrafter.
DR   CDD; cd08397; C2_PI3K_class_III; 1.
DR   CDD; cd00870; PI3Ka_III; 1.
DR   CDD; cd00896; PI3Kc_III; 1.
DR   FunFam; 3.30.1010.10:FF:000002; Phosphatidylinositol 3-kinase catalytic subunit type 3; 1.
DR   FunFam; 2.60.40.150:FF:000171; Phosphatidylinositol 3-kinase VPS34; 1.
DR   FunFam; 1.10.1070.11:FF:000014; Phosphatidylinositol 3-kinase, root isoform; 1.
DR   FunFam; 1.25.40.70:FF:000012; phosphatidylinositol 3-kinase, root isoform; 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; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 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; IPR057756; PI3-kinase_type3/VPS34_cat.
DR   InterPro; IPR015433; PI3/4_kinase.
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   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|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000587};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000587};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000886595};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT   DOMAIN          14..177
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          274..449
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          532..798
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   813 AA;  93303 MW;  F4A7CDA4CF20E784 CRC64;
     MGASEFRFFL SCDLNSPVTF RIEKLDGILP LHKSSDSGVV SGVEDKRPEL YIECALYIDG
     APFGLPMRTR LNTTGPPYCW NELITLSSKY RDLTAHSQLA ITVWDVSCGK AEGLIGGATI
     LLFNSKMQMK SGKQKLRLWQ GKEADGSFPT STPGKVPRHE RGELERLEKL MNKFERGQIQ
     SIDWLDRLML RSLDKIKEQE SSKHGNSYLY LVVDFCSFEH RVVFQESGAN LLITSPIGST
     NEFVTVWDTE LGKFNPSEHK QLKLARSLDR GIIDRDLKPS NNERKSIQRV LKYPPTRTLS
     GDERQLLWKF RFSLMSEKRA LTKFLRCVEW SDVQEAKQAI QLMYKWETID VCDALELLSP
     LFESEEVRAY AVSVLERADD EELQCYLLQL VQALRFERSD RSRLSQFLVQ RALQNIQLAS
     FFRWYVAVEL TDHVYNKRYF STYDLLEQSM KKLPPDVNGE DGNKLWQSLV GQTGLTAQLV
     SITREVRNVR GNTQKKIEKL RQLLSGLLSE LTYFEEPIRS PLTPSVLIKG IVPGESTLFK
     SQLNPLLLAF RTEDEGSCKV IFKKGDDLRQ DQLVVQMVWL MDRLLKLENL DLCLTPYKVL
     ATGHDEGMLE FIPSRSLAQI LSEHRSITSY LQKFHPDEHA PFGITATCLE TFIKSCAGYS
     VITYILGIGD RHLDNLLLTD DGRLFHVDFA FILGRDPKPF PPPMKLCKEM VEAMGGAESQ
     YYTRFKSYCC EAYNILRKSS NLILNLFYLM AGSTIPDIAS DPEKGILKLQ EKFRLDMDDE
     ACIHFFQDLI NESVSALFPQ MVETIHRWAQ YWR
//
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