ID A0A0R3PEF7_ANGCS Unreviewed; 429 AA.
AC A0A0R3PEF7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Lysosomal acid phosphatase {ECO:0000313|WBParaSite:ACOC_0000244901-mRNA-1};
GN ORFNames=ACOC_LOCUS2450 {ECO:0000313|EMBL:VDM54035.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000244901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000244901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM54035.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM54035.1,
RC ECO:0000313|Proteomes:UP000267027};
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; UYYA01000496; VDM54035.1; -; Genomic_DNA.
DR STRING; 334426.A0A0R3PEF7; -.
DR WBParaSite; ACOC_0000244901-mRNA-1; ACOC_0000244901-mRNA-1; ACOC_0000244901.
DR OMA; QESDWPQ; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; 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; ACID PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR11567:SF210; INTESTINAL ACID PHOSPHATASE; 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:UP000267027};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..429
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040667998"
SQ SEQUENCE 429 AA; 49508 MW; 4D79BF2D3F049D02 CRC64;
MTWFFLWCCL VSYFSFVNAE DEIPTGPPIP VTVRELKSGD TLLFVQVVWR HGDRAPTMTY
PTDVYQEDAW PNGWGELTQM GMRQQYALGQ VLRRRYIDID EPFISHRYNS KQVYFRSTDV
NRTLVSAYAN IAGMFTSGEP GKDYPAQESW PTGWTPVPVH TIPLEEDYVG NVFAPCPRAE
QLDNQLRNSV EFQAIKKSNE EFLQFLSEKT GMKVDLTNLY LINDVHYIET IYNMTQPDWL
TPEVSERLRN LTLVVNEYTY GIAKPYLPEL IRLRGGSMLR SIVDLIGQKL YCHRYVNERD
ECDWIRPLKY YAYSAHDTTV AALLTTFGDE EAVIRGGLPK YTASVAVELW MLEEGPAVRI
LFHGAFHHNY HTITHLTKGC PEDNEFCPLK VSFDPIVSLA STSFYFLQNF LRGLILMILK
FLFALFPTE
//
