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Database: UniProt
Entry: A0A2H3K2J8_WOLCO
LinkDB: A0A2H3K2J8_WOLCO
Original site: A0A2H3K2J8_WOLCO 
ID   A0A2H3K2J8_WOLCO        Unreviewed;       449 AA.
AC   A0A2H3K2J8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Phosphoglycerate mutase-like protein {ECO:0000313|EMBL:PCH43274.1};
GN   ORFNames=WOLCODRAFT_103320 {ECO:0000313|EMBL:PCH43274.1};
OS   Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phaeolaceae; Wolfiporia.
OX   NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH43274.1, ECO:0000313|Proteomes:UP000218811};
RN   [1] {ECO:0000313|EMBL:PCH43274.1, ECO:0000313|Proteomes:UP000218811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-104 {ECO:0000313|EMBL:PCH43274.1,
RC   ECO:0000313|Proteomes:UP000218811};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   EMBL; KB468135; PCH43274.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3K2J8; -.
DR   OMA; YIWNAAE; -.
DR   OrthoDB; 2786306at2759; -.
DR   Proteomes; UP000218811; Unassembled WGS sequence.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF195; ACID PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G14570)-RELATED; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000218811};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..449
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013763111"
SQ   SEQUENCE   449 AA;  50557 MW;  7040FA57975EEA32 CRC64;
     MVLLARLLLR LCLAFLLQST LLATTISQDY SGSLSSRAGV YNSSHTPEDL PWNTYNYCNA
     PHVNAEHYQM PSNVSNATLT YMNVVLRHHK RTPDNLYPEE NELNSVAWNC TGFHQFSYGG
     ESAMIYHKTY SPPWHPFLIQ IWNGTCDQGQ LTQEGLQDAI RHGEDLWAVY AEKLGFLTTI
     NEYDIFIRTS TETRTFQVAG GLLQGMDPGM ATKTFPVTTQ PSVIDSIPPD YSCPKADIIR
     SAFQSVPAWL AHLEKNAALQ ERLGTTLGTT GLSAWTSWYD HYFDTFTSRT CHGHPLPCNA
     TGACVSEQDA ARVFAIGDFE YNYIWNAAEN ATKYSQLTFG VFYMELAYNF KLFRSGGETH
     KLRLYVGHDG TMIRLASLLG IGRVAPLRWP AMGSEIVMEV WRTTDGEHFV RIMHEGTPVS
     GLEWQSLDDF IDALESQIPE NLYDECMEG
//
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