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Database: UniProt
Entry: A0A0N4ZDI3_PARTI
LinkDB: A0A0N4ZDI3_PARTI
Original site: A0A0N4ZDI3_PARTI 
ID   A0A0N4ZDI3_PARTI        Unreviewed;       595 AA.
AC   A0A0N4ZDI3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=AcidPPc domain-containing protein {ECO:0000313|WBParaSite:PTRK_0000564600.1};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000564600.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000564600.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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DR   AlphaFoldDB; A0A0N4ZDI3; -.
DR   STRING; 131310.A0A0N4ZDI3; -.
DR   WBParaSite; PTRK_0000564600.1; PTRK_0000564600.1; PTRK_0000564600.
DR   Proteomes; UP000038045; Unplaced.
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}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..595
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005891702"
FT   TRANSMEM        311..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        356..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        430..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        463..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        494..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          364..509
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   595 AA;  69447 MW;  FD8C6DEBC5723318 CRC64;
     MLTYKFVFLL LLVKIKNCHS LTIEESRKIL GLHYQEVQNG AKINNVTNED IEKKMGYVED
     EKLIERTTIT EEIEKEYENN VTILPEQIQE KDIKDNSKLQ FSLSESLTPM SENVDTGMEL
     MDGDGTETKE PDEKESPTIF EELFIDTLTQ RLNKQKKKFF NTNFENLPVE ESFETLSRLC
     YRFLQHYRYF CVNQIITPQN EMRCRGYRQD CSQFFRPKTP LERITEKYQS NIRLGYYKLN
     DMQKSMSPFI KNPGMTNISV SRILCDFLVL LLCATPLLIF HEFVKPYKRG FYCDDESIRY
     PYRPSTVTRQ MLIVVGILIP TFLIFATEIF RYTAWERKCA HVFKSYSLKN HRVNRLFVRL
     YTFLGYFFLG VCFNQIMVDI AKYTIGRHRP HFMDVCKPNK GYDVCPQDHS YINDFTCTGN
     DKYLIHESQL SFYSGHSAFS FYGAWYTSLY LQARLYKPLH SRILLPVIQF ALFGGASFVA
     YSRVSNYKHH WSDVLVGAIM GSAIGIFNAV CFAEVFKRRE IPPCDVALLT NDIEMEEGRS
     TNVDQSKFVS GVNKGSHQFK PISQDNHMKE RQDKINEHVP TFVNPNVPPL ATTEA
//
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