ID   A0A078AUW8_STYLE        Unreviewed;       485 AA.
AC   A0A078AUW8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Major acid phosphatase map (Histidine-acid phosphatase) {ECO:0000313|EMBL:CDW84663.1};
GN   Name=Contig10346.g11038 {ECO:0000313|EMBL:CDW84663.1};
GN   ORFNames=STYLEM_13729 {ECO:0000313|EMBL:CDW84663.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW84663.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW84663.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW84663.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) 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; CCKQ01013042; CDW84663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078AUW8; -.
DR   EnsemblProtists; CDW84663; CDW84663; STYLEM_13729.
DR   InParanoid; A0A078AUW8; -.
DR   OMA; YDFENIW; -.
DR   OrthoDB; 5477542at2759; -.
DR   Proteomes; UP000039865; 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; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..485
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001729711"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   485 AA;  56384 MW;  974077DFF686296D CRC64;
     MFNSILILLA FQSINLSNAK EQLEMAIEIC RHGARSPVDQ KHNVSQIYWP RGLGMLTEVG
     SRQQFELGTE LRKRYIDEYK LLDEVYNPEQ LLVMSTVRER CFESAQAQLQ GLYPPLTQSS
     QNTPKLTSWQ QTHVTLPLSS NDEDFKNFEN SDSLKNLNDS PGEIAYQNIP IYVQEEKKDF
     VLRGFSHKTC PIMVQRLQEA SQTQYYQDLL KYYQEKLFIP LSRKLNIQPE IMKWDEFQKM
     ADEIVLTLEN GQKLPFQLTE DELKLIRIFM ADEFFNVKNY GQDIPWFTSS RLREFIADKM
     QGKLNNEHNQ KFIIMSSHDS VVAMILAALD LRQDEQPKLA STVIFELWSS SNLTSINGNL
     PLQSKVQWVK LLYNDKELNL HTFCYGSSNS NNFMPNKCDF QTFQQKLSEN IYPIEKDCFE
     TQYSSIFQPL GQLDFGKYNQ TIVAVALLGF LVVLLVIGKK MFDNSLKKKQ PKKNFKGGFK
     FVETE
//