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Database: UniProt
Entry: A0A0A1TX84_ENTIV
LinkDB: A0A0A1TX84_ENTIV
Original site: A0A0A1TX84_ENTIV 
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
//
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