ID A0A0A1TX84_ENTIV Unreviewed; 846 AA.
AC A0A0A1TX84;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Phosphatidylinositol 3-kinase, putative {ECO:0000313|EMBL:ELP85883.1};
DE EC=2.7.1.153 {ECO:0000313|EMBL:ELP85883.1};
GN ORFNames=EIN_133870 {ECO:0000313|EMBL:ELP85883.1};
OS Entamoeba invadens IP1.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP85883.1, ECO:0000313|Proteomes:UP000014680};
RN [1] {ECO:0000313|EMBL:ELP85883.1, ECO:0000313|Proteomes:UP000014680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP1 {ECO:0000313|EMBL:ELP85883.1,
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.
CC {ECO:0000256|PIRNR:PIRNR000587, ECO:0000256|PROSITE-ProRule:PRU00879}.
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DR EMBL; KB207027; ELP85883.1; -; Genomic_DNA.
DR RefSeq; XP_004185229.1; XM_004185181.1.
DR AlphaFoldDB; A0A0A1TX84; -.
DR EnsemblProtists; ELP85883; ELP85883; EIN_133870.
DR GeneID; 14884865; -.
DR KEGG; eiv:EIN_133870; -.
DR VEuPathDB; AmoebaDB:EIN_133870; -.
DR OrthoDB; 6863at2759; -.
DR Proteomes; UP000014680; Unassembled WGS sequence.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR008290; PI3K_Vps34.
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; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 3.
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 ATP-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000587};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000014680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 1..85
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 128..290
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 309..487
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 552..832
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 846 AA; 98304 MW; E5D89C41E787F500 CRC64;
MKTIIHLPTD TISFVIKELH TKLYNSNPAV FPENSRDVDF VLKVRGLNEF LIPEKSDGGE
YVLSDFDYVR RCVHENLPID LVLYDRNKLH ERLWKADQIG LMGHLNTFIG SEVKALSDKT
RYLSQRDLKT PMCVEITQLD NFKYTKATDK MNFSVNFKCF ITGSLYYGVN LLAKEEVSPI
FEIENGRIKF NSPLVLTFNI LISSIPRETK IVLSVYYTDL SATGVPPELS KRQECLATIN
SKLIDYNGFF IRTKFRCGMW ERVEPNPINM CCENTSNEAC SIQFKLIEFN KPVIMDTFTA
TDDEMKTQMA SEIKLKAEDV IIYKKAVEAD PMAELTTEEI RMLWTYRAMV MKTKPRALSR
VVRAVDFSDQ EEVLELHRLL QKWPLIEPSH ALELLDFHYP DEEVRIYALK CIDAMKDYEL
VDFLPQLIQA LKFELHHLST LADFLLRRAL RNKNVIGHQF FWFLKAEVHD PRVTERYGTL
LEAFLNGIEG YRSELYNEVH LQNQLVTLAN QVKAISTKED QKAHLKSSLN KYNYPNEMSL
PLDSRLRVKR TVPNTGNVFS SKKKPLMLVW ENLDPLGKNI LVIQKVGDDL RQDVLTLQML
RLMNNIWKSA GLDLRMLPYQ CMATGNEMGM LELVEDSETY GAIIAKEEGT FRVFKDDVLT
KWMKEQCNRP ESKVTFDQAV ENFVYSCAGY CVATYILGIG DRHSDNVMIR RDGRFFHIDF
GHFLGNFKSK FGVKRERTPF KFTPHFAHVM GGKGSKMFKK FEELCISAFT CIRKQGSLFI
YLFRLMLATG IPELQKEKDI EYMRDTFMFD KKEDEAGEEF RQLIYKCLDA KSQTFNDLVH
DYVHYK
//