ID   A0A183AVN9_9TREM        Unreviewed;       282 AA.
AC   A0A183AVN9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=AcidPPc domain-containing protein {ECO:0000313|WBParaSite:ECPE_0001105801-mRNA-1};
GN   ORFNames=ECPE_LOCUS11024 {ECO:0000313|EMBL:VDP87961.1};
OS   Echinostoma caproni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC   Echinostoma.
OX   NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0001105801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ECPE_0001105801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP87961.1, ECO:0000313|Proteomes:UP000272942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Egypt {ECO:0000313|EMBL:VDP87961.1,
RC   ECO:0000313|Proteomes:UP000272942};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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; UZAN01050090; VDP87961.1; -; Genomic_DNA.
DR   WBParaSite; ECPE_0001105801-mRNA-1; ECPE_0001105801-mRNA-1; ECPE_0001105801.
DR   Proteomes; UP000050740; Unplaced.
DR   Proteomes; UP000272942; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd03384; PAP2_wunen; 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:SF103; FI04477P-RELATED; 1.
DR   PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000272942};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        162..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        217..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          91..235
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   282 AA;  31852 MW;  A695418AF60658DC CRC64;
     MSVCALCPMF FVLLSVSIPF TKNIRFLVFI AMGVLQNIEP YRKGYFANDE SIQYPYHSST
     VPIITVIIIF HHFQIVVVEL IIVLYAIYNH LIVSFFGYFL TIAITDVGKV AVGRMRPNFR
     DVCQPTPTST TILGYIFPYT CTKGTTKEQR DIXDILKSFP SGHSSTAMYS AIFLCIYFQL
     RWPRLGTPAI RVGLQAVCVS LGLAVCLSRI VDNKHHWSDV LSGSTIGTLI AITVVRILVS
     DNLFYFRLVD RLYTFAILSS IDPVYRFLGT LPNHESVLQE RA
//