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Database: UniProt
Entry: A0A0V1NT04_9BILA
LinkDB: A0A0V1NT04_9BILA
Original site: A0A0V1NT04_9BILA 
ID   A0A0V1NT04_9BILA        Unreviewed;       422 AA.
AC   A0A0V1NT04;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Lysosomal acid phosphatase {ECO:0000313|EMBL:KRZ87113.1};
GN   Name=acp2 {ECO:0000313|EMBL:KRZ87113.1};
GN   ORFNames=T08_13939 {ECO:0000313|EMBL:KRZ87113.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ87113.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ87113.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ87113.1};
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:KRZ87113.1}.
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DR   EMBL; JYDM01000105; KRZ87113.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1NT04; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT   REGION          400..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  48707 MW;  2FA1388F799BE625 CRC64;
     MNAAVKCVAI RFIVVVIVFA LPSEEALRLV QVVWRHGARA WLENTFLNCS HSSEYGAGEL
     SQVGFMEQYE LGQFLHERYK NFLSEFKMDE IYVRSTDTNR TILSALVNLA GLFPQNSNDS
     ALHLNWQPIP VHSVPKDNDP HFTFYSIVHF AFKLLYAFSK CKKVDDIYWN EVMTSAPVLK
     LMHQYAELFD LLRKQTGFPL KTLDDIYQVY EPLYSLVNEK KMSFKLIQTI NMQIQNDGFL
     PCLPEWLTVE LYQIIENLYR VSTTFYYNDQ RIKPYRGGIL LEHIANQIRK KIFGSIPKAK
     YFGYSTHDLT LIGLLENLNV YNAENHPEFS AALMVELHET STHGYTVELW YRTSLNNNTL
     KQLFIPECSP TCSAEEFLNF SKGKGVADWF EGCESLPSTT TSTMQDVNHS DLQTGKNYPS
     HK
//
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