ID   A0A0V1MGP2_9BILA        Unreviewed;       424 AA.
AC   A0A0V1MGP2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Putative acid phosphatase 5 {ECO:0000313|EMBL:KRZ70789.1};
GN   Name=pho-5 {ECO:0000313|EMBL:KRZ70789.1};
GN   ORFNames=T10_5961 {ECO:0000313|EMBL:KRZ70789.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ70789.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ70789.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ70789.1};
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:KRZ70789.1}.
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DR   EMBL; JYDO01000107; KRZ70789.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1MGP2; -.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..424
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006882535"
SQ   SEQUENCE   424 AA;  48751 MW;  16657ECC39378036 CRC64;
     MIAAVKCVAI HFIVVVIVFA LPSEEALRLV QVVWRHGARA SLENTFLNCN HSSEYGAGEL
     SQVGFMEQYE LGQFLHERYK NFLSEFKMDE IYVRSTDTNR TILSALVNLA GLFPHNSNDS
     ALHLNWQPIP VHSVPKDNDP HFGFYSIVHF AFKLLYTFAK CKKVDDIYWN EVMTSAPVLK
     LMHEHAELFD LLRKQTGFPL KTLDDIYQVY EPLYSLIKND GFLPCLPEWL TVELYQIIEH
     LYRVSTTFYY NDQRIKPYRG GILLEHIANQ IHKKILGSIP KAKYFGYSTH DLTLIGLLEN
     LNVYNAENHP EFSAALMVEL HETSTHGYTI ELWYRTSLNN NTLKQLFIPE CSPTCSAEEF
     LNFSKDKGVA DWFESCESLL STTTTSTTHD MNQSDLQIRK NYRRHKLSSL SSLSISKADP
     QITG
//