ID   Q68HW1_9PLEO            Unreviewed;       874 AA.
AC   Q68HW1;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   Name=bgl1 {ECO:0000313|EMBL:AAU00986.1};
OS   Parastagonospora avenae f. sp. avenae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=215456 {ECO:0000313|EMBL:AAU00986.1};
RN   [1] {ECO:0000313|EMBL:AAU00986.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SAA001NY-85 {ECO:0000313|EMBL:AAU00986.1};
RA   Ueng P.P., Reszka E., Malkus A., Chung K.-R., Bergstrom G.C.;
RL   Submitted (JUL-2004) 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   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|ARBA:ARBA00004987}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336}.
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DR   EMBL; AY688370; AAU00986.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q68HW1; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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:SF12; BETA-GLUCOSIDASE A-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 {ECO:0000256|ARBA:ARBA00023277};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..874
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004269579"
FT   DOMAIN          791..859
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   874 AA;  94439 MW;  AA9557F6357555DB CRC64;
     MALASTLVAF FVTQVLGQQY PTSNTSSPAA NSSSPLDNAV SPPFYPSPWI EGLGDWEAAY
     QKAQAFVSQL TLLEKVNLTT GTGWQSDHCV GNTGGVPRLN FTGICNQDAP LGVRFADYVS
     AFPSGGTIAA AWDRGEWYLR GYQMGSEHRS KGVDVQLGPV VGPLGRNPKG GRNWEGFSPD
     PYLSGIASAE SVRGIQDAGV IACTKHYIMN EQEHFRQPGN FEDQGFVDAL SSNLDDKTLH
     ELYLWPFADA VRAGTGSIMC SYNKVNNSQA CQNSYLQNYI LKGELGFQGF IMSDWDAQHS
     GVASTFAGLD MTMPGDTDFN SGKTFWGTNF TTSILNGTVP QWRLDDAVTR IMAAFYYVGR
     DKARIPVNFD SWSRDTYGFD HYYGKAGYSQ INSHVDVRAD HFRSIRRTAA MSTVLLKNEG
     ALPLTGSEKW TAVFGDDAGD GQLGPNGSPD HGGNNGTLAM GWGSGTSDYP YLVTPLESIK
     ATVAQNGGVV TSVTDNWAYT QIQTLAKQAS VAIVFVNADS GEGYITVDGN AGDRNNLTLW
     QDGDTLIKNV SSLCNNTIVV IHSVGPVLVN SFYDSENVTA ILWAGLPGQE SGNAIADILY
     GRHNPGGKLP FTIGSDAAEY GPDLIYEPTN NSSSPQDNFE EGVFIDYRAF DKQNVTPIYE
     FGFGLSYTKF SYSNLTVKKA NAGAYTPATG QSKAAPTLGN FSTDASQYQW PSDFTYVDTF
     IYPYLNSTDL KTASQDPEYG LDYTWPAGAT DGTPQARIPA GGAPGGNPQL WDVLFSVEAT
     ITNNGTLPGD EVVQLYVSLG NPDDPKIVLR GFDRLSIQPG KTATFHADIT RRDVSNWDVA
     SQNWVITSAP KTVYVGASSR KLPLTATLDT SDFQ
//