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Database: UniProt
Entry: M2R7W4_CERS8
LinkDB: M2R7W4_CERS8
Original site: M2R7W4_CERS8 
ID   M2R7W4_CERS8            Unreviewed;       464 AA.
AC   M2R7W4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Phosphoglycerate mutase-like protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CERSUDRAFT_86207 {ECO:0000313|EMBL:EMD34786.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD34786.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD34786.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD34786.1,
RC   ECO:0000313|Proteomes:UP000016930};
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA   Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA   Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA   Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA   Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA   Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA   Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA   Martinez A.T., Vicuna R., Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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; KB445802; EMD34786.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2R7W4; -.
DR   STRING; 914234.M2R7W4; -.
DR   HOGENOM; CLU_030431_3_1_1; -.
DR   OrthoDB; 5486499at2759; -.
DR   Proteomes; UP000016930; 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:UP000016930}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   464 AA;  51753 MW;  BCB9039CB8BC1127 CRC64;
     MALHASGAPT GTTHTTLGLT NATPGHVPLD VEGYPIAPPE LELEQVHMYV RHGERTPVGV
     RMAAPPASIP EHWMFCNTAR QFRAAVAGGH GWFASDASQL EPNEDESLRT RRIVERRDGT
     PAQGECLLGE LTDVGRESTY NLGSSLRELY VNKLGFLPDV VHSNDEVYFR STNMPRTIES
     LQQVIHGLYP TTKAAEDFTP LVRVRNGKDE NLFGNTLACK RLEILQIGFA QAAVAAWNPS
     LEPLDKKVSK YLQGPIRLDG KPRASGVLDT IRAADAHGIP VPHEFKEKGV LDVIEKAVVQ
     EWFADKTEEV RRLGMGPLLS DLSSKMQRKA ELGGQDPLKI LVHSTHDTCL AGLCSTLDAY
     DEKWPAFAAS ITFELFRKRP DETQRSSYWQ TILSPFRRPQ PVEHYVRMRY QNRNLPLPFC
     SEKGKHLHGA PEFCTLAAFR ERVAELTPKD WEAECAISSN RTTN
//
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