ID   B0EPD2_ENTDS            Unreviewed;      1071 AA.
AC   B0EPD2;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform, putative {ECO:0000313|EMBL:EDR23615.1};
DE            EC=2.7.1.153 {ECO:0000313|EMBL:EDR23615.1};
GN   ORFNames=EDI_083720 {ECO:0000313|EMBL:EDR23615.1};
OS   Entamoeba dispar (strain ATCC PRA-260 / SAW760).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370354 {ECO:0000313|Proteomes:UP000008076};
RN   [1] {ECO:0000313|Proteomes:UP000008076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC PRA-260 / SAW760 {ECO:0000313|Proteomes:UP000008076};
RA   Lorenzi H., Inman J., Schobel S., Amedeo P., Caler E.;
RT   "Annotation of Entamoeba dispar SAW760.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00879}.
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DR   EMBL; DS550224; EDR23615.1; -; Genomic_DNA.
DR   RefSeq; XP_001739975.1; XM_001739923.1.
DR   AlphaFoldDB; B0EPD2; -.
DR   EnsemblProtists; EDR23615; EDR23615; EDI_083720.
DR   GeneID; 5885131; -.
DR   KEGG; edi:EDI_083720; -.
DR   VEuPathDB; AmoebaDB:EDI_083720; -.
DR   eggNOG; KOG0904; Eukaryota.
DR   OMA; CIRAFAC; -.
DR   OrthoDB; 6863at2759; -.
DR   Proteomes; UP000008076; Unassembled WGS sequence.
DR   GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00891; PI3Kc; 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; IPR000341; PI3K_Ras-bd_dom.
DR   InterPro; IPR035448; PI3Kc.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10048:SF14; LD28067P; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00794; PI3K_rbd; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   SMART; SM00144; PI3K_rbd; 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   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51547; C2_PI3K; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EDR23615.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDR23615.1}.
FT   DOMAIN          203..302
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          346..513
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          532..710
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          775..1057
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1071 AA;  125404 MW;  5083A2224BCA3FA6 CRC64;
     MCSRLTRTTF SVPRVTGTTS VLRKNIPVIR VIVENEGKTF TPINTPQQII NFYYDPKKTK
     EKYYFCLNHQ PYYFDRLSEP FFECKFCIYC NSYGYWPTFT LVKVEQCINY KPINSFLNFL
     ESNKMTFDCI GNEFLLVLKA NTDECRDFRA TLARILQEKI VLFESDVIDK FGDDTQSQQD
     AKDIYEENEY VYVESEPPIP TNCIELKING RYGVDMSMKT IVQKPTDTIA KVINNLFTKL
     YTMKPKIFDK NSKATDFVLK VRGSNEFLIP YNNDKIEYTL NDFDYIRKCV RLNQNIDVVL
     FNRKKMYQYM FDKEKIVLLK QFNTFVGNDY WSKLQKNTND LSQRAAQIQF SIQIISIENI
     KYLKIIKKED KKETISITSF RAYFALSLHY GIRYLEKEKF TNVFQVSEGK LLLKEPFNVS
     FETLLSSLPK ETKMIISLYM TELPVGISVN EINKKDICLA TINCKLVDHH KYFMKGLFNV
     GMWERTEPNP IMMCCENTSP ETCKLRYCVI EFDKPIKMDT FIGTEEEMNV PINTSQKLDL
     NDTKIFKEAV EADPLTVLSQ EDCRLLWKYR YLVEKTKPGS LARLVSAVDF TQQSEVLELH
     RLLNKWPLLK PTQALELLDF RFPDEQVRLF ALKCLDAMKD YELVNFLPQL VQALKFELHH
     QSNLAYFLLR RALRNKNIIG HQFFWFLKAE MHDNRVTERY GVLLEAFLNG CENYRTELYN
     EVTFQNQLVV IANKVKQIEV KEEQKQLLKD SLAKLKYPEE MSLPLDSRFR IKKPVPNTGN
     VFSSKKKPLM LVLENVDPLG DNIMVIQKVG DDLRQDVLSL QMIQLMNNIW KSAGLDLRML
     PYHCTATGNE IGMLELVQDS ETYGKIIADE GGQGTLRICK EDLLTKWLKK QCSRKESKVT
     FEQAVENFTY SCAGYCVATY ILGVGDRHSD NVMIRRDGRF FHIDFGHFLG HFKSKFGVKR
     ERTPFKFTQH FAHVMGGKGS TQFSIFEDLC IRAFACIRKQ GSLFIYLFRL MLATGIPELQ
     HEKDIEYMRD TFMFDKKDDE AKEAFRQLIY ECLEAKSQTL NDMIHDFVHY K
//