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Database: UniProt
Entry: A0A016RZK6_9BILA
LinkDB: A0A016RZK6_9BILA
Original site: A0A016RZK6_9BILA 
ID   A0A016RZK6_9BILA        Unreviewed;       455 AA.
AC   A0A016RZK6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Histidine acid phosphatase {ECO:0008006|Google:ProtNLM};
GN   Name=Acey_s0329.g2674 {ECO:0000313|EMBL:EYB83798.1};
GN   ORFNames=Y032_0329g2674 {ECO:0000313|EMBL:EYB83798.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB83798.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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:EYB83798.1}.
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DR   EMBL; JARK01001665; EYB83798.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016RZK6; -.
DR   STRING; 53326.A0A016RZK6; -.
DR   Proteomes; UP000024635; 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:SF207; 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:UP000024635};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..455
FT                   /note="Histidine acid phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001488759"
SQ   SEQUENCE   455 AA;  51946 MW;  F030ABDF27550397 CRC64;
     MHSCRLSSQV INRKTKTGML IILSLLLSPA IALKDGEMEL LLVQVIWRHG DRSPTYTFRS
     DPFQERNWTF GGGGYGQLSP IGMKQHFNLG KLIRNMYVDT GFLGGRYSSK EIYVRSSDLN
     RTIISAMSNM MGMYGQNDSI RGVDYPDVPG WPVGYVPVAV HTVNRNTDYV VIPHAPCDRQ
     EKLWKMAKES DEVKAYLNKP EVANVFRDLT SKCGEEIDTE NIWIVRDALL IEQIHANETL
     RKTNKWFSDE FFKKISEIDV QLQQYGNGIF SKPVIMNNLD IGLEIQKIRG GSMFNDLNMH
     MNMKLDCLNN KHRPRCKWIS GLKYYVYSGH DTTISAFFSI LRLEEVIIPR GYPAYSAAVF
     IELWMNTTDG QPYFKIAYHP DDVENSIYPV TQRIAACEGK IYCNLAVFRD YAAKIKPDQA
     MYKWCRVDPL KASAALLSLA TLALSLISQA SWLSY
//
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