ID M2S4T8_ENTHI Unreviewed; 638 AA.
AC M2S4T8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Phosphatidylinositol4,5-bisphosphate 3-kinase catalytic subunit gamma, putative {ECO:0000313|EMBL:EMD46326.1};
GN ORFNames=EHI5A_179140 {ECO:0000313|EMBL:EMD46326.1};
OS Entamoeba histolytica KU27.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=885311 {ECO:0000313|EMBL:EMD46326.1, ECO:0000313|Proteomes:UP000011755};
RN [1] {ECO:0000313|EMBL:EMD46326.1, ECO:0000313|Proteomes:UP000011755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KU27 {ECO:0000313|EMBL:EMD46326.1,
RC ECO:0000313|Proteomes:UP000011755};
RA Hannick L., Zafar N., Lorenzi H., Ali I.A., Petri W.P., Caler E.;
RL Submitted (FEB-2013) 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; KB444575; EMD46326.1; -; Genomic_DNA.
DR AlphaFoldDB; M2S4T8; -.
DR EnsemblProtists; EMD46326; EMD46326; EHI5A_179140.
DR VEuPathDB; AmoebaDB:EHI5A_179140; -.
DR Proteomes; UP000011755; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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 Gene3D; 2.60.40.150; C2 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; 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; IPR015433; PI_Kinase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF14; LD28067P; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL 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 SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EMD46326.1};
KW Transferase {ECO:0000313|EMBL:EMD46326.1}.
FT DOMAIN 155..254
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 298..465
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 484..638
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
SQ SEQUENCE 638 AA; 75268 MW; 31E732AAA5943F6D CRC64;
MRSRLTRTTF SVPRVTGTTS LLMKNIPAIR VIVENEGKTF TPINTPQQII NFYYDPKKTT
EKYYFCLNHQ PYYFDRFKVE QCTNYKPINI FLNFLESNKI TFDCIGNEFL LVLKANTDEC
RDFRATLARI LQEKIIYEEN EYVYVESEPP IPTSCIELKI NGRYGVDMSM KTIVQKPTDT
IAKVINNLFT KLYTMKPKIF DKNSKPSDFV LKVRGSNEFL IPYNNDKIEY ILSDFDYIRK
CVRLNQNIDV VLFNRKNMYQ YMFDKEKILF VKQFNTFVGN DYWNKLQKNT NDLSQRVAQI
QFSIQIISIE NIKYLKTIKK EDKKETISIT SFRAYFVLSL HYGIRCLEKE KYTNVFQVND
GKLILKEPFN VSFETLLSSL PKETKMTISL YMTELPVGIS INEINKKDIC LATINCKLVD
HHKYFMKGLF KVGMWERTEP NPIMMCCENT SPETCKLHYC VIEFDKPIKM DTFIGTEEEM
NVPINTSQKL EVSDTKRFKE AVEADPLTVL SQENCRLLWK YRYLVEKTKP GSLARLVSAV
DFTQQSEVLE LHRLLNKWPL LEPTHALELL DFRFPDEQVR LFALKCLDAM KDYELVNFLP
QLVQALKFEL HHQSNLAYFL LRRALRNKNI IGHQFFWF
//
