ID   BGLG_ASPTN              Reviewed;         817 AA.
AC   Q0CUC1;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   22-FEB-2023, entry version 64.
DE   RecName: Full=Probable beta-glucosidase G;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase G;
DE   AltName: Full=Cellobiase G;
DE   AltName: Full=Gentiobiase G;
DE   Flags: Precursor;
GN   Name=bglG; ORFNames=ATEG_02713;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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 (By similarity).
CC       {ECO:0000250}.
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   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; CH476596; EAU37675.1; -; Genomic_DNA.
DR   RefSeq; XP_001211891.1; XM_001211891.1.
DR   AlphaFoldDB; Q0CUC1; -.
DR   SMR; Q0CUC1; -.
DR   STRING; 341663.Q0CUC1; -.
DR   GlyCosmos; Q0CUC1; 14 sites, No reported glycans.
DR   EnsemblFungi; EAU37675; EAU37675; ATEG_02713.
DR   GeneID; 4317206; -.
DR   VEuPathDB; FungiDB:ATEG_02713; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_3_1; -.
DR   OMA; YERGYAM; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   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   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..817
FT                   /note="Probable beta-glucosidase G"
FT                   /id="PRO_0000394118"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        402
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        563
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        584
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        623
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        662
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        679
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        715
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   817 AA;  88407 MW;  C3D3219F884364C1 CRC64;
     MANIAHLIVS GLLAATVAHG QQYEGSSRSE DAFSYVQPRN TTILGQYGHS PAVLPSPNST
     GSGGWQAAHT KARHFVSQLT LEEKADMVTG QPGPCVGNIV AIPRLGFNGL CLQDGPLAIR
     VADYASVFSA GVTAASTWDR DVLYERAFAM GQEFRAKGAH IALGPVAGPL GRSAYGGRNW
     EGFAADPYLT GVAMELSVKG YHDAGVQATP KHFIGNEQET QRNPIYNPNG TITDVLQEAV
     SSNIDDRTMH ELYLWPFANA AHAKAAAFMC SYQRLNGSYA CQNSKALNGL LKEELGFQGY
     VMSDWGGTHS GVASIESGLD MNMPGGLGPY GTIPQAGSFY GGNVTQGVKN GTIDEARVDD
     MIIRIMTPYY WLGQDKDFPS VDPSSADLNT FSPRSTWLRQ FNLTGERNRD VRGDHAKIIR
     RQAAEATVLL KNEKNALPLK SPKSLAIFGN DAGEPTMGAV NQANFEFGTL AAGGGSGTGR
     FTYVVSPLEA IQSRAKQANT LVQYWMNNTD IATTDVTTLW VPAPPDACLV FLKTWAEEGE
     DREYLHVDYD GNDVVSSVAS KCNNTIVVTH SSGINELPFA DHPNVTAILA AHYPGQESGN
     SIVDVLYGDV NPSGRLPYTI ARNGSEYNAP PTTEVTTTGA EDWQAWFNEK LEIDYRYFDA
     HNISVLYEFG FGLSYTTFNL SEINAEPLVE SISSVPEQRP IQPGGNPALW ENVYNVSVVV
     TNTGDVEGKA VPQLYVTFPD STPAGTPPKQ LRGFDKVALK PGQSQAASFQ LMRRDLSYWD
     VVSQQWLIPE GEFVISVGFS SRDLREVVRV TPVSGST
//