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Database: UniProt
Entry: A0A0V0VWD0_9BILA
LinkDB: A0A0V0VWD0_9BILA
Original site: A0A0V0VWD0_9BILA 
ID   A0A0V0VWD0_9BILA        Unreviewed;       393 AA.
AC   A0A0V0VWD0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Lysosomal acid phosphatase {ECO:0000313|EMBL:KRX67752.1};
DE   Flags: Fragment;
GN   ORFNames=T09_15027 {ECO:0000313|EMBL:KRX67752.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX67752.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX67752.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX67752.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX67752.1}.
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DR   EMBL; JYDN01000004; KRX67752.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0VWD0; -.
DR   Proteomes; UP000054681; 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; 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.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        358..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX67752.1"
SQ   SEQUENCE   393 AA;  45645 MW;  45C39E91C1BC848D CRC64;
     LKGQSFLQMW RHGARAPLTL FPSEYDHTIQ NWPNGLGELT PLGILQQFQL GTFLRQRYEK
     LIPKYKSDTI YIRSTDSNRT IMSAMANLAG MFPPENSQNI LNLTWQPIPI HTIPKTLDKV
     LDVTYSTCPY PDHVFYSEEM NSETVRAIME EKAAIFDFLR ERTGLEIPTF TDIFDVYDLL
     NCEKAHNMVE TNRTWMNEAL FKEIEDLFLK STLHYYSNSK ITPFRGGPLL QSVAEVLMKK
     AKKIYNEQLK YMAYSAHETG IIAFFTSMQI YNTSLIPDFA ACIMTELYEE EDGTYTVDIL
     YKRSLKEEVQ ILELPWCGTV CNLETFINWS NNIAVKDWEK ECGLRREENF SELQQRRAVI
     FLSVALIVVI TGLCILSVMY YQLKKLIKLK IPD
//
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