ID A0A0K6G2J3_9AGAM Unreviewed; 776 AA.
AC A0A0K6G2J3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Probable beta-glucosidase G {ECO:0000256|ARBA:ARBA00039579};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase G {ECO:0000256|ARBA:ARBA00041276};
DE AltName: Full=Cellobiase G {ECO:0000256|ARBA:ARBA00041601};
DE AltName: Full=Gentiobiase G {ECO:0000256|ARBA:ARBA00041808};
GN ORFNames=RSOLAG22IIIB_10267 {ECO:0000313|EMBL:CUA72730.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA72730.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA72730.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA72730.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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}.
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DR EMBL; CYGV01001308; CUA72730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K6G2J3; -.
DR Proteomes; UP000044841; 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; 3.20.20.300; Glycoside hydrolase, family 3, N-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; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_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; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000044841};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..776
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005502912"
FT DOMAIN 695..765
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 199..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 83495 MW; 130F55E53921E743 CRC64;
MRGAFLASSL ALYFNLSVAS RGERRQTNNG TWSGPLADGG NAWKDAFAKA KQVVSQMTLE
EKVNLTTGVG TSSVCAGNTG AVPRFNIPSL CLQDGPAGVR PADFASQFPA QVTVGATWDR
ELIYERAAAL GAEFRGKGIH VALAPVTGGP LGRSPLGGRN WEGFSSDPYL SSVGSYLSVK
GFQDKGVVAT SKHYAVYEQE TKRNPNSPSS AEHPLPISSD VDDATFHETY LPSFVEAVRA
GTGAIMCCYN RINGSHGCED DVSLNQILKG ELDYQGYVMS DWFAHWTNEG AALGGMDMTM
PGTGFWGVDL VAMVNNGTVP ATRLDDMVHR ILTPYYALGQ DKGFPDVQYN TGGITGDSYL
STNPGNTNVN VQADHYKIIR KIGEDSATLL KNVRTNGGGL PLKKSEFVAV FGQDAGANPD
GLLACGSINQ CATEHANNGT VSTGGGSGAA FAPYIVTPLE GIQSRTKADS TQVNWMLNDL
DLATAKTNAI IADTSIVFTY SYQTEFVDRD NLTLWSNGDA LINTVAAECN NTIVVIHSGQ
QVLMESWINN PNVTAVVFAY YPGQETGNAI ASILYGEVNP SGKLPFTLAK SLSDYPPNGI
YTENMADPHV VFEEGNLIDY RWFDAKNVTP RFEFGFGMSY TTFSYSGIKL QSTPGKPTDG
VQLTKEPFDG KATLYDVAYT VTASVKNTGS VSGCEVAQLY LSYPASQTKQ PVRSLRGFDK
LCLNKGQTKT ATFKLRQKDH AVWDVVRQTW TIPKGVFTVY VGSSSRTLPL KTTFTV
//
