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Database: UniProt
Entry: A0A366QNU8_9HYPO
LinkDB: A0A366QNU8_9HYPO
Original site: A0A366QNU8_9HYPO 
ID   A0A366QNU8_9HYPO        Unreviewed;       880 AA.
AC   A0A366QNU8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=FIESC28_10999 {ECO:0000313|EMBL:RBR06604.1};
OS   Fusarium coffeatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR06604.1, ECO:0000313|Proteomes:UP000253153};
RN   [1] {ECO:0000313|EMBL:RBR06604.1, ECO:0000313|Proteomes:UP000253153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR06604.1,
RC   ECO:0000313|Proteomes:UP000253153};
RA   Gardiner D.M.;
RT   "Fusarium incarnatum-equiseti species complex species 28.";
RL   Submitted (JUN-2018) 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}.
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:RBR06604.1}.
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DR   EMBL; QKXC01000342; RBR06604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366QNU8; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000253153; 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; 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   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361161};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361161}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..880
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016867297"
FT   DOMAIN          781..855
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   880 AA;  95568 MW;  E450A47AE172D82B CRC64;
     MTVAKVAALA LANFAALGSS APAKGSDGFI AAPYYPAPYG GWVDDWADSY AKAKELVDSM
     TLAEKTNITS GTGIFMGNPC NGNSGSADRV GFPQLCLNDA ANGVRQTDNV TVFPDGITAG
     ATFDKKLIYE RGAAIGKEAR GKGVHVWLGP SVGPLGRKPK GGRNWEGFGT DPALQAIGAR
     ETIKGVQENG VVATIKHLIG NEQEMYRRQT TDVVSPAYSA NIDDRTMHEL YLWPFAEAVR
     AGVGAAMTAY NRVNGTMSSE HSYLINALLK EELGFQGFVM TDWLSQITGV ASAIAGMDMS
     MPGDPIIPLL GNSLWMYEMT RATLNGSVPM ERLNDMATRV VATWYKFGQD QDDFPKVNFD
     TNTNEAVGPL YPGAWPNSPK GVVNKFVQVQ EDHDVIARQV AQDAITMLKN DNNLLPLSKK
     SPIKVFGTGA QTNPDGPNAC PDRNCNKGTL GQGWGSGTVN YMYLDDPIGA IKDEAGDVTF
     YNTDKFPSVP SATDDDVAIV FVTSDAGENS YTVEGNNGDR SKDKLNVWHG GDNLIKAAAE
     KYKNVIVVIH TVGPVLLEQW HDMPSVKAVL VAHLPGQEAG KSLTNILFGD ASPCGHLPYS
     ITKKEDDMPE SVTKLIDSGF VDPPPDTYSE KLYIDYRWLN KEKIRPRYAF GHGLSYTNFT
     YSNATIKRVT KLSQYPPSRS AKGEVLDYAQ DIPDYKEAVK PKDFKTVWRY LYSWLSESDA
     KKAAEAAGKS KYPYPEGYST KQKTSLPRAG GAQGGNPALW DEAYTISVRV TNSGAKYAGK
     ASVQAYVQFP EAAGYETPII QLRDFEKTAV IEPGESETVE LTLTRKDLSV WDVAAQDWLV
     PKPDGEYKVW LGGASDALDV VCYTDDLSCE NDVDGPVSYD
//
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