ID   A0A316ZA47_9BASI        Unreviewed;       487 AA.
AC   A0A316ZA47;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Phosphoglycerate mutase-like protein {ECO:0000313|EMBL:PWN97135.1};
GN   ORFNames=FA09DRAFT_330775 {ECO:0000313|EMBL:PWN97135.1};
OS   Tilletiopsis washingtonensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC   Tilletiopsis.
OX   NCBI_TaxID=58919 {ECO:0000313|EMBL:PWN97135.1, ECO:0000313|Proteomes:UP000245946};
RN   [1] {ECO:0000313|EMBL:PWN97135.1, ECO:0000313|Proteomes:UP000245946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4186 {ECO:0000313|EMBL:PWN97135.1,
RC   ECO:0000313|Proteomes:UP000245946};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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; KZ819296; PWN97135.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316ZA47; -.
DR   STRING; 58919.A0A316ZA47; -.
DR   OrthoDB; 5486499at2759; -.
DR   Proteomes; UP000245946; 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:UP000245946}.
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  53047 MW;  9FEB7E12B178982A CRC64;
     MATSSSSASS ASPLASSSQG PLDSARGRAS ASLGFEAPPA HLALAQVHYL VRHGERTPVR
     TRLTNSNPAI PARWNFCHAG RQFATAVSDL TPTEGAHRLP AGPWQKKGEE QWSGTMRVAK
     GTESTKRDTP VPGEEGECLL GELTDLGRAS TFQLGAALRA LYIDQLQLLP SRLSPQDAEA
     VYFRSTNMSR TIESCQSLIR GLLPQTREKE DAFTPTILVR NGTDENLLPN TFGCARLRVL
     DGQFAAFAAS QHASHLATFD AAVAPHCDGT LPRVDGHPRL NGIVDTIRAA QAHALPVPKV
     FERPDVVEAF ETAVVDEWFT GYKAQDEALR KQYRRLAMGR LLGDLQGRMQ SKAEKGEQEK
     LKLALYSAHD TSLAGLLSTL DVFEQRWPSF TASVGIELWR DTRASAQPSL LSFLGLGRST
     TQHYVRMRYG DSTLRLPACA GKGQHLDGKP EFCTLEAFGE AVEALRHEGG KTWEEECEEG
     RGAKSSK
//