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Database: UniProt
Entry: A0A0K0ES84_STRER
LinkDB: A0A0K0ES84_STRER
Original site: A0A0K0ES84_STRER 
ID   A0A0K0ES84_STRER        Unreviewed;       412 AA.
AC   A0A0K0ES84;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   SubName: Full=AcidPPc domain-containing protein {ECO:0000313|WBParaSite:SSTP_0001231200.1};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|Proteomes:UP000035681, ECO:0000313|WBParaSite:SSTP_0001231200.1};
RN   [1] {ECO:0000313|Proteomes:UP000035681}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SSTP_0001231200.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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DR   AlphaFoldDB; A0A0K0ES84; -.
DR   STRING; 6248.A0A0K0ES84; -.
DR   WBParaSite; SSTP_0001231200.1; SSTP_0001231200.1; SSTP_0001231200.
DR   Proteomes; UP000035681; 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:SF114; ACIDPPC DOMAIN-CONTAINING PROTEIN; 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:UP000035681};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        243..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        274..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          143..289
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          391..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  47616 MW;  AB561099894BAFC0 CRC64;
     MSVPPSRAQS EVFSASQYGG KIRRPRYLIN YFVLPTFIVH VIGLACLWTL WYYLRFTDVF
     PYHHRVFYCQ DIHLMLPNFK PEDFNVYVSY ELLYVLAFCL PPLVILLGEV AFWLFSTKPR
     KTIYASFGEC KVHLFTRRLF RFISVFLFGA LITQIFVDSI KLLTGYQRPY FLSLCNVNMA
     ACTAPLQYSP SPSPHLACNY KGASELRYAW LSFPSLHAAF SSYSAIFASC YIYYMINLRG
     APLLRPFLIF GFLGLTLVDA FSRINGYKNH WRDIWVGWLI GFVIAFFLCY CVLCFQEVYH
     YVIERPPVAV TQGEGGGVAV PEERVSPFFS WFRLPRVQAP SVKEEYVVYE EDVPQVSTVP
     NGAPSRHRKG HDRTCEITTV TESYHRTIIP PGQQRERERE HSQANMSAYG AY
//
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