ID A0A074RD02_9AGAM Unreviewed; 234 AA.
AC A0A074RD02;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=V565_324010 {ECO:0000313|EMBL:KEP45056.1};
OS Rhizoctonia solani 123E.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP45056.1, ECO:0000313|Proteomes:UP000027456};
RN [1] {ECO:0000313|EMBL:KEP45056.1, ECO:0000313|Proteomes:UP000027456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=123E {ECO:0000313|EMBL:KEP45056.1,
RC ECO:0000313|Proteomes:UP000027456};
RA Cubeta M., Pakala S., Fedorova N., Thomas E., Dean R., Jabaji S., Neate S.,
RA Toda T., Tavantzis S., Vilgalys R., Bharathan N., Pakala S., Losada L.S.,
RA Zafar N., Nierman W.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose.
CC {ECO:0000256|ARBA:ARBA00024983}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEP45056.1}.
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DR EMBL; AZST01002309; KEP45056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074RD02; -.
DR STRING; 1423351.A0A074RD02; -.
DR HOGENOM; CLU_004542_0_1_1; -.
DR OrthoDB; 1659294at2759; -.
DR Proteomes; UP000027456; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF19; BETA-GLUCOSIDASE G-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KEP45056.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027456}.
FT DOMAIN 152..222
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 234 AA; 26045 MW; AD08A1A9A15872D7 CRC64;
MESWIDNPNV TAVVFAYYPG QETGNAIASV LYGEVNPSGK LPFTLAKSLS DYPPNGIYTE
NVTDPHVVFE EGNLIDYRWF DAKNVTPRFE FGYGMSYTTF DYSNIKLRST PGKPTDGVQL
TKEPFDGNAT LYDVAYTVTA SIKNTGSVSG CEVAQLYLSY PASQTKQPLR SLRGFDKLCL
KKGQTKTATF KIRQKDHAVW DVVRQTWTIP KGEFTVYVGS SSRALPLRTT LKVS
//
