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Database: UniProt
Entry: A0A024TU19_9STRA
LinkDB: A0A024TU19_9STRA
Original site: A0A024TU19_9STRA 
ID   A0A024TU19_9STRA        Unreviewed;       489 AA.
AC   A0A024TU19;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Histidine acid phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=H310_09428 {ECO:0000313|EMBL:ETV97508.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV97508.1};
RN   [1] {ECO:0000313|EMBL:ETV97508.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV97508.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) 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; KI913972; ETV97508.1; -; Genomic_DNA.
DR   RefSeq; XP_008873717.1; XM_008875495.1.
DR   AlphaFoldDB; A0A024TU19; -.
DR   STRING; 157072.A0A024TU19; -.
DR   EnsemblFungi; H310_09428-t26_1; H310_09428-t26_1-p1; H310_09428.
DR   EnsemblProtists; ETV97508; ETV97508; H310_09428.
DR   GeneID; 20086478; -.
DR   VEuPathDB; FungiDB:H310_09428; -.
DR   eggNOG; KOG3720; Eukaryota.
DR   OrthoDB; 5477542at2759; -.
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; 2.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..489
FT                   /note="Histidine acid phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013062472"
SQ   SEQUENCE   489 AA;  54349 MW;  BF97CB6709D180FD CRC64;
     MAKAAAVAFA QVALASMYDG WSVPDYCMAT DTMTKVAIQP VTTTRSMELV QAQVVARHGA
     RAPYSRVFCW ETAASPVNAV WNCSTSSVWS EDIASPSNKN RGYGRLYKKQ YLDGENVLPG
     TCAVGGLLPL GRQQHRRVGE FLRDAYIGHG PHKLFASSKL NTIPKHQLYL RSDDEERTLG
     SGHALVDGLF PYDPSDDVDA EHMLTWMTTD GATDYIDHKN DTSCPVLPYI VEQVQASPEW
     TSSAASVAAL QAAFERVVNG TFSWDTCLEC LMIARCNDLA LPPGTTQDMF DGLIQHVQAR
     KKLVLTYRDG WYAKVDMHRM WADVLHRMDA AMANPEDAPK LAITIGHDST IMPMMAVLLG
     DRWDGGWTTY AGTLVFELYK EEKRQIDDTS AYAVRVVYNG YPLQLPFCLD DLCDWTVFNE
     TLAFARGARS CLVPTTTSPP LPHVQLWKPH GLHWAAAAIM FGASAAMTVA MMRELRHRHE
     DPTTRYLLG
//
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