ID A0A0A1UEI9_ENTIV Unreviewed; 1078 AA.
AC A0A0A1UEI9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform, putative {ECO:0000313|EMBL:ELP94903.1};
DE EC=2.7.1.153 {ECO:0000313|EMBL:ELP94903.1};
GN ORFNames=EIN_249470 {ECO:0000313|EMBL:ELP94903.1};
OS Entamoeba invadens IP1.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP94903.1, ECO:0000313|Proteomes:UP000014680};
RN [1] {ECO:0000313|EMBL:ELP94903.1, ECO:0000313|Proteomes:UP000014680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP1 {ECO:0000313|EMBL:ELP94903.1,
RC ECO:0000313|Proteomes:UP000014680};
RA Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL Submitted (OCT-2012) 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; KB206169; ELP94903.1; -; Genomic_DNA.
DR RefSeq; XP_004261674.1; XM_004261626.1.
DR AlphaFoldDB; A0A0A1UEI9; -.
DR EnsemblProtists; ELP94903; ELP94903; EIN_249470.
DR GeneID; 14893900; -.
DR KEGG; eiv:EIN_249470; -.
DR VEuPathDB; AmoebaDB:EIN_249470; -.
DR OrthoDB; 6863at2759; -.
DR Proteomes; UP000014680; 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; 3.10.20.770; -; 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:ELP94903.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELP94903.1}.
FT DOMAIN 185..285
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 363..526
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 535..713
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 778..1058
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1078 AA; 124107 MW; B184C9F19CC031BA CRC64;
MSRKLLRSSV AVKSTVSESV VHVVFKKDDH VYIYTFPATS TAFGIKNAIK SEMKLEGTYS
IVIPSIPFKV VDAMEDTVIK EMGFYDTCVK FGLFPTFEMV NREIAESYES VAGLSKLMTK
LSANYQTIGQ NYVDVLRTDV EEIFVFRRSL ARVRLISNSL EEKYDRKIHE ENEYAYTLSE
PNLPTSVNKL DIRVVGTDLN LTAVFKVTPD VKVQKFINAI YVEFMKKSPM KMSGYNTTSF
VLKVMGYDEY IIPKKVDGKE WLLSDFDYIR RQGIRGESLQ LELVPRDNLL KCMISEEDVK
TMKYLDTFFA SEYWEAFDEE KRCSQRQCTD QFSMVITSVE NLVYLSKKKG NKSKKEKKEK
EEEESTLIVK DENQEDEEVE RVTDFLGYIS AELFYGEISL CPAIYSPVFE IKNGLANPKW
KATFVQLLAT LPAESKVIYS VYKTDKVVNT VVTEVSEEDK CVGTVNTRVV NYLNDLISGA
QQYTLWQSEP NPIAMCCNAV SSQEKLCVEY PILTNPVRMD TFITKKKEME TNMCSQNQQP
MGVDEVNAFN KIVHADALAV FTKEELKCLW EQRYTILKSK PQALARLLNS VNYTQPSEVH
EMHRLLARWP LLQPEEAIEL LDFRYPDPQI RAFALRCIDT MTDDQLVMYL PQLVQALKFE
LHHHSALASF LLRRSLKNRR RIGHNFFWFL KAEIHDARVT ARYGVLLEAF LVGCGNYKVE
LEKEVVFQSQ LVVIANEVKD VANKDEQTEL LKSSLGKLKY PDEMSLPLDS RFRIKKTVPN
TGKVFSSKKK PLMLVLQNAD PLGEAIVVIQ KVGDDLRQDI LTLQMIRLMN GIWKNNGLDL
CMLPYLCIAT GNEIGMLELV KNSETYGKIM AMDEKKLSVF RETAMTTWLK DQCSSPDSKV
QFELAVENFT YSCAGYCVAT YILGIGDRHS DNVMLTKEGK FFHIDFGHFL GNFKKKFGVK
RERTPFKFTP HFANVMGGKG SPQFKKFEKV CIDAFITIRQ HGPLFIYLFR LMLATGIPEL
QKVNDIEYMR NMFMFDKNDQ EAGEEFRKLI YKCLDAWSQT FNDAVHDFVH YKKLPMFK
//
