ID   A0A165N781_EXIGL        Unreviewed;       303 AA.
AC   A0A165N781;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:KZW00321.1};
GN   ORFNames=EXIGLDRAFT_722372 {ECO:0000313|EMBL:KZW00321.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW00321.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZW00321.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZW00321.1,
RC   ECO:0000313|Proteomes:UP000077266};
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   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000256|ARBA:ARBA00038362}.
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DR   EMBL; KV425902; KZW00321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165N781; -.
DR   InParanoid; A0A165N781; -.
DR   OrthoDB; 1456057at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   CDD; cd07040; HP; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR   PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..303
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007863023"
SQ   SEQUENCE   303 AA;  33224 MW;  79B2515561EA7227 CRC64;
     MKFARVCVAL GAAAGALAAA VEASSSAGST FTYEVVTGIF KQDDPTIPPA EIGATPASFG
     LIDESPLRWL KLKAKILSLN LFAPRNTQYK LLFLGRHGEG WHNVAEAFYG TPAWDETWSK
     LDGNGTIVWG PDAQLTPLGE AQAANVTLLW EKELQAGIPI PEILYSSPMS RAAKTARISF
     EWLWKTGKRA LILENFREVI GVHTCDERKT KTYIQEQFGD IMNIEKGFTE QDELWTADHR
     ETNDEQNVRL KKALDFVFSH GGTYVSVTAH SGALNAAFRV MGHRDYGIPT GGVVPVLLKA
     TKA
//