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Database: UniProt
Entry: A0A016V318_9BILA
LinkDB: A0A016V318_9BILA
Original site: A0A016V318_9BILA 
ID   A0A016V318_9BILA        Unreviewed;       405 AA.
AC   A0A016V318;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Histidine acid phosphatase {ECO:0008006|Google:ProtNLM};
GN   Name=Acey_s0020.g227 {ECO:0000313|EMBL:EYC21108.1};
GN   Synonyms=Acey-pho-5 {ECO:0000313|EMBL:EYC21108.1};
GN   ORFNames=Y032_0020g227 {ECO:0000313|EMBL:EYC21108.1};
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:EYC21108.1, 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:EYC21108.1}.
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DR   EMBL; JARK01001356; EYC21108.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016V318; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   405 AA;  46071 MW;  50146086906056EE CRC64;
     MAEAWQAPLE ANTTTLVYVQ VAWRHGDRTP ATPVPFSGAD SWSEGLGELT KKGIAQQYRL
     GKWLRARYGK FLGDRFDRHE VFVRSSDYNR TLMSAQANMA GLFPPSKSEI WETGLAWQPV
     PVHSIPKSID KELYEDIACP TASAEFRKVW KSGVVSKMEL ENEDLILFLR EHSQIPNFQF
     YMLWMIYDNL FCMLQHNDTH VWPPWMNSSL FSRVQKLYDA SSRMKYHTEV LRRLRGGPLL
     KDVIDRFVAK RNGDLGDRPK LYAYSAHDTT LAAMLSTLGI YPAEFPRYAT AVLLELHSRD
     GELVIEVYHK NMTDVDSVYR YSIPGCPDPC TLDALRSTVE KYLPNDWTAE CGLAGPDALN
     YMISTAVFAC TTVLLAGFIA LDVTLKRRHR SSFASDPLMV DDDEA
//
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