ID   A0A1Y2F2Z1_PROLT        Unreviewed;       424 AA.
AC   A0A1Y2F2Z1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Histidine phosphatase superfamily {ECO:0000313|EMBL:ORY78251.1};
GN   ORFNames=BCR37DRAFT_400382 {ECO:0000313|EMBL:ORY78251.1};
OS   Protomyces lactucae-debilis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC   Taphrinales; Protomycetaceae; Protomyces.
OX   NCBI_TaxID=2754530 {ECO:0000313|EMBL:ORY78251.1, ECO:0000313|Proteomes:UP000193685};
RN   [1] {ECO:0000313|EMBL:ORY78251.1, ECO:0000313|Proteomes:UP000193685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12-1054 {ECO:0000313|EMBL:ORY78251.1,
RC   ECO:0000313|Proteomes:UP000193685};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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}.
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:ORY78251.1}.
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DR   EMBL; MCFI01000018; ORY78251.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2F2Z1; -.
DR   STRING; 56484.A0A1Y2F2Z1; -.
DR   OMA; SWPPFTS; -.
DR   OrthoDB; 5486499at2759; -.
DR   Proteomes; UP000193685; 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: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.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000193685}.
SQ   SEQUENCE   424 AA;  47549 MW;  C24BE3851610DFB7 CRC64;
     MSLHPDVHIT TYNDAKLAEL YPEHLSLRLV QILFRHGERT PVRQRLPSAG LPLQYRMCFN
     AERFRAAVKM TNGWNELPYA RRLEVPANTR SGSGLSTAAA LPGTCLLGEL TDRGRQSTFY
     LGERLKELYV DRLGFAKISH ESELYLRASP IPRALESLQH VFSGMFPRSS LPKQFELIIH
     QRDWTQENLY PNEGACKRLQ QLAKEYAKRA ALTWNPILAG HASELLSEKY LDGKPLQVDG
     NPRVTGLADT INAAIGNGLD IPAEFRDKDM LKQVEAAAVE EWFGGYLADE AYRRLGAGRL
     LGDFRDRMVM CAGRESSLKV ALYGAHDTTI GAVLASLGVF DRRWPPFSSH IAIELFEDAR
     ASSDSITGES HLVRLRYNDK VLHIPGCTEA VHGFCTLKEF NKVIDELVPE DWEAECRAKP
     DLSA
//