ID M2R9A0_CERS8 Unreviewed; 447 AA.
AC M2R9A0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Phosphoglycerate mutase-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CERSUDRAFT_157771 {ECO:0000313|EMBL:EMD35002.1};
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:EMD35002.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD35002.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD35002.1,
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 -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; KB445801; EMD35002.1; -; Genomic_DNA.
DR AlphaFoldDB; M2R9A0; -.
DR STRING; 914234.M2R9A0; -.
DR HOGENOM; CLU_030126_0_0_1; -.
DR OrthoDB; 2786306at2759; -.
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; 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:UP000016930};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..447
FT /note="Phosphoglycerate mutase-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004024636"
SQ SEQUENCE 447 AA; 49958 MW; 3B7D1A5A11215734 CRC64;
MSRQWKAWCA LLLQIPLNIG FSTPAHAEDA LATKNGVYDS STTPTNLPWN TYNYCNAPHL
NAEHYSKPDN VTDPKLVFLN VVMRHHKRTP DNLYPNENEL NAIPWNCTNF HQFSYGGGSA
QIYHETFSPP WHPFLSQMWN GTCDEGQLTE EGLQDAIKHG KDFWSVYAHE LGFLDSVNTK
DIFVRTSTET RTFQTAGGML VGMDPGMATK TFPVVTQPSP IDSIPPDYSC PKADDIRDAF
QPVPAWNNHL EENMDLQNSL TALTGTTGMT AWTSWYDHFF DTFTSRTCHG HPLPCNSSGA
CVSEDQAAQV FAIGDFEYNY IWNAAVNASA YTQLSFGVFF MELVHNFKAF RSGSETRKLI
LYVAHDGSMI RLASGLGLGK VAPLRWPALG SEISMEVGQY APDNSHFVRV IHEGTPVPGF
EWIPLDSFID NLDEQVPADL FNTCMEG
//
