ID M2QFH4_ENTHI Unreviewed; 1047 AA.
AC M2QFH4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Phosphatidylinositol4,5-bisphosphate 3-kinase catalytic subunit delta, putative {ECO:0000313|EMBL:EMD48049.1};
GN ORFNames=EHI5A_034560 {ECO:0000313|EMBL:EMD48049.1};
OS Entamoeba histolytica KU27.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=885311 {ECO:0000313|EMBL:EMD48049.1, ECO:0000313|Proteomes:UP000011755};
RN [1] {ECO:0000313|EMBL:EMD48049.1, ECO:0000313|Proteomes:UP000011755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KU27 {ECO:0000313|EMBL:EMD48049.1,
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; KB444160; EMD48049.1; -; Genomic_DNA.
DR AlphaFoldDB; M2QFH4; -.
DR EnsemblProtists; EMD48049; EMD48049; EHI5A_034560.
DR VEuPathDB; AmoebaDB:EHI5A_034560; -.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMD48049.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 183..283
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 326..501
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 510..688
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 753..1033
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT COILED 494..521
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1047 AA; 120412 MW; 711FAE45FF277469 CRC64;
MKKSVHSSVV NSQSQGSIVH VFIRHEGEIH SFTYSSTVSP LDIIDSIKST LHLTGVYSVV
VPNIPFKIVD SMEGSEVKET GFYKSCTEYG IIPAFELIER SQAEKYESVG ILAKLMNQLK
ENYQIIGQTY VDVLNTDAEE IFVFRRSLAR TRVLSSKIEA KYDSNLKEEN EFAYTLSEPN
IPDTIKSIDV EIIGEDYKTT AIFSITPQVF VYRVIDSAFN ELKKAGEGVV NGKEPSEYIL
KVVGWDEYIV PQRVNGKNWL LSDYDYIRRC ALHGEAVHLE LVKKSRLFSC KINDEERKVL
NYLDSFFASE LWEAFDDEKR VSQRLCTDQL SAQVVSVENL CSYIKTKKGD EEEQQMITDF
LCYFKVELYY GEKSLCPALY STVFEVKNGL ASPKWKFTFI QLIATLPAET KMIYSVYMTN
SIVNTQIEKI GENDKCLGTV NTKIVNYTND LLNGEQQYYL WASEPNPIAM CCNAVSSKMK
VVVEFPSLTK PIRMDTYITK KKEMQVELEQ ESEKKMTVEE LDAFKKIVDA DAMAVFTQEE
LKCLWERRYS LLKTNPHALA RLLNSVNYCQ PTEVHELHRL LSKWPLLDPR EAIELLDFRY
PDPQIRGFAL RCIDTMTDDQ LVMYLPQLVQ ALKFELHHHS TLASFLLERS LKNRRRIGHN
LFWFLKAEIH DARVTGRYGV LMEAFLNGCG RYKNELEKEV TFQNQLVVIA NEVKRLGTKD
EQKAHLKSSL AKLEYPDEMS LPLDARFRIK KPIPNTGNVF SSKKKPLMLV LENADPLGEP
IMVIQKVGDD LRQDILTLQM IRLMNTIWKN NGLDLCMLPY LCIATGNEIG MLELVKNSET
YGAIMAMDKS KFSVIKDTAV TTWLKEQCAR PESQVTFQEA VENFTYSCAG YCVATYILGI
GDRHSDNVMI SRDGKFFHID FGHFLGNFKS KFGVKRERTP FKFTQHFANV LGGKGSPQFV
KFEEICMNAF VIIRKHGPLF IYLFRLMLAT GIPELQSAKD IEYMRNMFMF DKNDDEAKEA
FRQLIYKCLD AWSQTVNDLI HDFVHYK
//
