ID B0E9B7_ENTDS Unreviewed; 250 AA.
AC B0E9B7;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Phosphatidic acid phosphatase type 2 domain containing protein, putative {ECO:0000313|EMBL:EDR28881.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:EDR28881.1};
GN ORFNames=EDI_301510 {ECO:0000313|EMBL:EDR28881.1};
OS Entamoeba dispar (strain ATCC PRA-260 / SAW760).
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370354 {ECO:0000313|Proteomes:UP000008076};
RN [1] {ECO:0000313|Proteomes:UP000008076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PRA-260 / SAW760 {ECO:0000313|Proteomes:UP000008076};
RA Lorenzi H., Inman J., Schobel S., Amedeo P., Caler E.;
RT "Annotation of Entamoeba dispar SAW760.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; DS548309; EDR28881.1; -; Genomic_DNA.
DR RefSeq; XP_001734945.1; XM_001734893.1.
DR AlphaFoldDB; B0E9B7; -.
DR EnsemblProtists; EDR28881; EDR28881; EDI_301510.
DR GeneID; 5879875; -.
DR KEGG; edi:EDI_301510; -.
DR VEuPathDB; AmoebaDB:EDI_301510; -.
DR eggNOG; KOG3030; Eukaryota.
DR OMA; HAYFRHM; -.
DR OrthoDB; 25293at2759; -.
DR Proteomes; UP000008076; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd03390; PAP2_containing_1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR PANTHER; PTHR10165:SF35; RE23632P; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:EDR28881.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..212
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 250 AA; 28089 MW; E1CBF9D3B51746F3 CRC64;
MNKILNVIFQ IGGDIIYLIF TGAIAAVFTF IDGFHMEVPG GENNVNVLYP YRDSTFSDLV
AAIVIYVSAI MIIFAFQIKR LSLRHFIFTY IGLGASVTTW LMFVQGGKIY AGRPRPNMYA
LVAQGKEKDA WKSFPSGHSA ASFCGYTYLS LYIAGELRIF IDRPELWRMI PVITPLLIAG
IIVLTRTRDY YHNFSDVLAG SIIGIFSACI GYFSKFESLF SPKAGEIRFT CRGHKKNNED
ISDEEMTEMS
//
