ID   A0A158Q8Q5_9BILA        Unreviewed;      1065 AA.
AC   A0A158Q8Q5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit {ECO:0000313|WBParaSite:EEL_0000840501-mRNA-1};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000840501-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000840501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00879}.
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DR   AlphaFoldDB; A0A158Q8Q5; -.
DR   STRING; 1147741.A0A158Q8Q5; -.
DR   WBParaSite; EEL_0000840501-mRNA-1; EEL_0000840501-mRNA-1; EEL_0000840501.
DR   Proteomes; UP000050640; Unplaced.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; cd05165; PI3Kc_I; 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; IPR003113; PI3K_ABD.
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:SF111; PHOSPHATIDYLINOSITOL 3-KINASE AGE-1; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF02192; PI3K_p85B; 1.
DR   Pfam; PF00794; PI3K_rbd; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   SMART; SM00142; PI3K_C2; 1.
DR   SMART; SM00143; PI3K_p85B; 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; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51544; PI3K_ABD; 1.
DR   PROSITE; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          24..113
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          194..295
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          338..490
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          510..697
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          763..1051
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1065 AA;  122677 MW;  134957FBF174729D CRC64;
     MQGVVCPQDS PDVWSFIECG QLEVEGSTVL DLLLPNGFLV NVRCSMDLTL AMLKQELFIQ
     AKKLPLFNLL LTPSDYIFFT IRTDGEREEL YDESRSIFSL RLFVPLLCLI EPEGNREEKE
     LIHDIGLAIG RPLTEIEAKL SSEEMSYRMD LYRVSEQAVS NRGVVGYSHY AFPEEVSSEL
     DADIPPQVKS KIQMADLYIE LWYRSREDEL ANIDTNCVCV KIRKVIGVHA SDAITNAIKE
     LMQQHKLFIK EAASDFLLQI AGRRCFLTKD IRLTSFEYVR SSFENYRIPK FILRRKDIVM
     KDFTESPPIT KPSWVRAYES RVDRGDEIAR KECSLWKVDD NLKLRIHSAS HLSILDFDKI
     YVKASLYHGI DLIANKESSY VSPSNPRWSD GWIDFDVYLK DLAPSTQLCL SLVAVKQKKK
     EEYSGIGWVN LRLFDCNGKL VQGKFMLYLW PFPKYCTELL HPSGQVGSND NRDTVRIEVE
     FQDYGCIEFP DLDSVCEYVE KLDIRCARSP LPPLSSPSGS MKEFLDSLHF VDAEYLTDKQ
     MEHLWEAREL VAQYKPDLLP LIARCPMIWT RRDEFSRLYE LLKRWGKIQP ETALMLLDFK
     YSDVRIREFA VDSLDNVLDN DRLQLYVLPL IQVLKFEPYG SCALSRMLLK RALCNNRIGH
     ILFWLLRAEL GQLSEVGQDL TKIYKRFALM IEAYCRANCA HLNSMLRQVD MVVRLTDLSK
     IIKTMKDNEC ATKHLQKELA SYVEIMQNMI SPLDISDSLG ALNIEQCKVI GSAKQPLRLA
     WTNPEPLARL HSETHQIIFK NGDDLRQDML TLQVMRIMDA LWKSQDYDLC LSIYEVLPMG
     RNVGMIYVVQ NCSTLFEIQC AAKQLGSTFS MESGLINKYI RNCSENSKVY LEGVDRFTAS
     CAGYCVATYV LGIKDRHQDN IMLAKDGRLF HIDFGHFLGH YKKKLGINRD RVPFVLTDHF
     LCVIAKGKSN FRDSHEYKKF KKLCTDAYII LHQRSKLFIS LFSMLLCTGL PELQKAGDID
     FLKGTLCSDM DSSHAATSFY KIFEEAFSGA WSTKTNWFFH SVKHL
//