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Database: UniProt
Entry: A0A0L6WKG8_9AGAR
LinkDB: A0A0L6WKG8_9AGAR
Original site: A0A0L6WKG8_9AGAR 
ID   A0A0L6WKG8_9AGAR        Unreviewed;       727 AA.
AC   A0A0L6WKG8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN   ORFNames=J132_02551 {ECO:0000313|EMBL:KNZ75609.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ75609.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU361161};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; KQ412607; KNZ75609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6WKG8; -.
DR   STRING; 1306850.A0A0L6WKG8; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000053712; Unassembled WGS sequence.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
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   InterPro; IPR019800; Glyco_hydro_3_AS.
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   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF2; BETA-GLUCOSIDASE L-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361161};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053712};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..727
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005569326"
FT   DOMAIN          161..385
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          435..681
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
FT   REGION          698..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   727 AA;  77528 MW;  2D8AF26723CA0679 CRC64;
     MFCHFLSFVI LDLLSGASGI EPLSSSLGSS APISASSASF SSVVSLQSRT AVSNLAPSSV
     IQSSVLASAA PSQSPISGLF PATDPKHPPS TQDSTEIVPD FAPAWSSAHS KAKAKIARFS
     LDELASVVTG VQSTGRPGRC VAITGRGWPG LCLEDSPLGV RLADFVTAFP TGINTAATFN
     RSLIRLRGLY MGLEHVGKGV NVALGPMMNL ARVAEGGRNF EGFGEDPFLA GEAAYETILG
     MQQGGVQACA KHFIDNEQEH NRMTSSSNVD DRTQHEIYAQ PFLRSVMAGA ASVMCSYNQI
     NGTYACENNK TLNDILKSEF GFQGFVVSDW GATHSTLSAV DGLDMTMPGN IGVGPGSFFG
     TNLTAAVHNR MISEDRLKDM ATRVLAGWYF LHQDSSSFPA VNFNANNPGD LATNEHIDVQ
     DDHFKIVREI GAASTVLLKN KNDALPLKRP RSIFLAGSDA GPAREAGPNA FRDQTGNDGI
     LAMGGGSGTA NFTYLISPYE ALQARARKDR TTVSWIFDDF NVARAGNMAI GTSAAIVFVN
     SDSREGSDRA NLTAWHEGDN LILAVAAQNN NTIVVVHSVG QLIVEPWIDH PNVTAVLWAS
     APGEEAGNSI TDVLYGDWNP SGRLPYTIAK RIEDYSAQVT LGGTPGTILQ IPYTEGLLIG
     YRGFDAHNIT PRFEFGFGLS YTKFEYSNLH ITKISSSSLS PTERAQEKNW DRGDSSSTGI
     GSSTALW
//
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