ID   A0A0V1CQ06_TRIBR        Unreviewed;       425 AA.
AC   A0A0V1CQ06;
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=Putative acid phosphatase 5 {ECO:0000313|EMBL:KRY51369.1};
GN   Name=acp2 {ECO:0000313|EMBL:KRY51369.1};
GN   ORFNames=T03_7271 {ECO:0000313|EMBL:KRY51369.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY51369.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY51369.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY51369.1};
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:KRY51369.1}.
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DR   EMBL; JYDI01000127; KRY51369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1CQ06; -.
DR   STRING; 45882.A0A0V1CQ06; -.
DR   Proteomes; UP000054653; 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:UP000054653};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        382..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   425 AA;  48638 MW;  93C5EB3FD470F1BD CRC64;
     MNAAVKCVAI RFIVVVIVFA LPSEEALRLV QVVWRHGARA WLENTFLNCS HSSEYGAGEL
     SQVGFMEQYE LGQFLHERYK NFLSEFKMDE IYVRSTDTNR TILSALVNLA GLFPQNSNDS
     ALHLNWQLIP VHSVPKDNDP LLYAFSKCKK VDDIYWNEVM TSAPVLKLMH QYAELFDLLR
     KQTGFPLKTL DDIYQVYEPL YSLIQNDGFL PCLPEWLTVE LYQIIENLYR VSTTFYYNDQ
     RIKPYRGGIL LEHIANQIRK KIFGSIPKAK YFGYSTHDLT LIGLLENLNV YNAENHPEFS
     AALMVELHET STHGYTVELW YRTSLNNNTL KQLFIPECSP TCSAEEFLNF SKGKGVADWF
     EGCESLPSTT TSTMQDVNHS DLVVILLSVC TGICCILLLL FVGILYNGKK ISPQQFANRE
     ELSKP
//