ID   A0A158QMK9_HAEPC        Unreviewed;       394 AA.
AC   A0A158QMK9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Acid phosphatase {ECO:0000313|WBParaSite:HPLM_0000867901-mRNA-1};
GN   ORFNames=HPLM_LOCUS8671 {ECO:0000313|EMBL:VDO35514.1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000867901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0000867901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO35514.1, ECO:0000313|Proteomes:UP000268014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHpl1 {ECO:0000313|EMBL:VDO35514.1,
RC   ECO:0000313|Proteomes:UP000268014};
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; UZAF01016908; VDO35514.1; -; Genomic_DNA.
DR   STRING; 6290.A0A158QMK9; -.
DR   WBParaSite; HPLM_0000867901-mRNA-1; HPLM_0000867901-mRNA-1; HPLM_0000867901.
DR   OMA; QESDWPQ; -.
DR   Proteomes; UP000038042; Unplaced.
DR   Proteomes; UP000268014; 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; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000268014}.
FT   REGION          367..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   394 AA;  45433 MW;  B2AD733133705299 CRC64;
     MTYPTDTHQE EAWPNGWGEL TELGMRQQYA LGNVLRRRYM GSANPFLDRR YNSKQVYIRS
     TDVNRTLISA YSNIAAMFAG GEPGKDFPNE TDWPTGWTPV PVHTLPGNED HAGNVFAPCP
     RAEQLDDELR NSKEYKQLAK DNEACDLLEY LSKNTGMKIE LPNVYLINDV HYIETIYNMS
     QPEWMTHEVS KRLRNLTSIV NEYTYGIGEP YLPELIRLRG GDCTKPTTCV PGPMLRSLVD
     LMNQKKECLD DSKQQNECKW IKPLKYYAYS AHDTTVAALL STFGDEEEVI RGGLPKYTAS
     VAVELWTLEG EGLAVRILFH GAFHHNYHII THLTKGCPVD KEFCPLEVFE KRSTQFMPVD
     MRKECERRQR SNRTNQTWEA RKMTEHRMNR KGFS
//