ID   A0A165YG98_9AGAM        Unreviewed;       426 AA.
AC   A0A165YG98;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Phosphoglycerate mutase-like protein {ECO:0000313|EMBL:KZV74189.1};
GN   ORFNames=PENSPDRAFT_573300 {ECO:0000313|EMBL:KZV74189.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV74189.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV74189.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV74189.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV424482; KZV74189.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165YG98; -.
DR   STRING; 1314672.A0A165YG98; -.
DR   InParanoid; A0A165YG98; -.
DR   OrthoDB; 5486499at2759; -.
DR   Proteomes; UP000077086; 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; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086}.
SQ   SEQUENCE   426 AA;  47226 MW;  CD5BC6289E9916A0 CRC64;
     MVLPQTKPKT GDKYRAPKTE LDVTGYPVAP EGLGLEQVHV YMRHGERTPV STRMTEFIPE
     RWLMCSQARR FNATVGDTDN STSALDITRV VERPDGRAVT GECFLGELTD VGRASTLAFG
     TALRRLYVER LGFLPDTLTD STSVYFRSTN MPRTVESLQQ AIHGLYPMSK CDANATHTLR
     VRNGREENLI GNTLGCKRLE TLLINFANAA ASAYNPTLEP LDKKVSKYLG DNPIRVDGRP
     RASGVLDTIR AAMAHDMKVP PEFEERAVSS VIERAVVNEW FSDKSEEVRR LGMGRLLGDI
     VEKMHLKTQS VNAAPKILVH STHDTGLAAL LNTLDVFDDR WPGFTASITF ELYKANKKPS
     TTAPPVDTAS AEAHVRARYS NRNLILPSCS EEGKHLPGSP EFCTLEAFTE RVSELVPNDW
     EAECST
//