ID   A0A0R3X3J8_HYDTA        Unreviewed;       441 AA.
AC   A0A0R3X3J8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Lysosomal acid phosphatase {ECO:0000313|WBParaSite:TTAC_0000792801-mRNA-1};
GN   ORFNames=TTAC_LOCUS7913 {ECO:0000313|EMBL:VDM32386.1};
OS   Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX   NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000792801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TTAC_0000792801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM32386.1, ECO:0000313|Proteomes:UP000274429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000032};
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   EMBL; UYWX01020420; VDM32386.1; -; Genomic_DNA.
DR   STRING; 6205.A0A0R3X3J8; -.
DR   WBParaSite; TTAC_0000792801-mRNA-1; TTAC_0000792801-mRNA-1; TTAC_0000792801.
DR   Proteomes; UP000046396; Unplaced.
DR   Proteomes; UP000274429; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274429};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..441
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5040668600"
FT   TRANSMEM        404..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   441 AA;  49838 MW;  D915EF4E9852AD6E CRC64;
     MILQWGLLFF LVTCLVDGLG GNESLLSVFI LARHGERYPC HILRHPGYPK EFMKMRCQLT
     ETGARQHFEL GRFIGRRYSS LLTWKGFKRN DVHIRSTGTE RTILSATYFG LGLDSSKEVK
     LPVLPAVFSS PKRHDYLLKM SYPCSAFDKL YEKALTSNLT RDFINRMRGL FDDLNNFTEF
     NFESDSLHKY LPKLWDLCES IHAWDKLERD TKGESLPFTS DLASACHRAL SFRQQLLFSS
     PAQTFFRGGP LWRHVLLTLK SRISPGEKNI LPLEIADIDA LDIPIVSDSR LFAYFAHDST
     LTAFLSHLGA FNNILPPYAS AVIVELHRLV HGELALRFFY HNESKLSPSQ LIPLTTELCG
     GKGAYWCPLE VLEDRLHGKA ATDMENACTA DETSSSSISL AASALAASIL FAFVLPIGFI
     IRVLLCLISI LLTYRFLFPI V
//