ID   A0A2H3TJJ1_FUSOX        Unreviewed;       848 AA.
AC   A0A2H3TJJ1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=FRV6_12940 {ECO:0000313|EMBL:SCO88813.1};
OS   Fusarium oxysporum (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO88813.1, ECO:0000313|Proteomes:UP000219369};
RN   [1] {ECO:0000313|Proteomes:UP000219369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA   Guldener U.;
RL   Submitted (SEP-2016) 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; FMJY01000007; SCO88813.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3TJJ1; -.
DR   VEuPathDB; FungiDB:FOC1_g10001894; -.
DR   VEuPathDB; FungiDB:FOC4_g10005227; -.
DR   VEuPathDB; FungiDB:FOIG_14378; -.
DR   VEuPathDB; FungiDB:FOMG_08823; -.
DR   VEuPathDB; FungiDB:FOXG_12989; -.
DR   VEuPathDB; FungiDB:FOZG_14688; -.
DR   VEuPathDB; FungiDB:HZS61_006900; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000219369; 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; 2.60.120.260; Galactose-binding domain-like; 1.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 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.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361161};
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}.
FT   DOMAIN          400..564
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   848 AA;  94478 MW;  62D4C65D6DE349EF CRC64;
     MPLLVDVDHA LKELTIEEKV KLLSGKDNWS TYPIERLNIP SLTATDGPHG ARGTSFFNGP
     LGALLPSATA MGATFDTRLM RSVGNMLAAE TIEKGCQILL APTVCLQRSP LIGRGFEAFG
     EDPILSGMMA SEYINGVQEK GVATSIKHYA AHDQSYRSPE DDLQVAERTL REVHLLPFQL
     AVKHANPWSF MTSYHRINGV HTSENEWLNT QILRREWGWD GLLMSDWGGV FSTAEAINAG
     LDLEMPGPSR WRGDLLHLAI FSRKVTKSMI NERVRNVVKL VNRVQPAFEH TTPNEEAGDT
     PKKRALCREV AQGSIVLLKN ERKVLPLDPS AQQTYGLIGP GVIYPAVSGG GSADLRPYYV
     RKPLEAIQDV VGREKVRTAI GCYSHIFTPP LSEYVTVPGT DEEGYQLFWY GEDPETNPEA
     EPLHSTTTTQ ATMYFADNHP SRVPDMYWLR LVTLYRATKT ATMHIGLCVM GKGRLYIDGK
     AAIDLWSSHP KKTLQTPMFN QASMELTADL EAHEGQVYEI SVLLKNESMS SNIGGPYVGT
     SCIGGVRIGC CEKIDPAVAL AEAVEVARNV DVPILIAGLN ADYETEAVDR HDLELPPGIN
     ELVRRVIEAN PKTIIVNQSG CPVTMPWANN ASTLVQVWFG GQETGNAIAD VLFGRYNPSG
     RLSITFPRRL EDTPSFLSFG KGVRHMYYGE GVFIGYRYYE KLRNDPLFYF GFGLSYTTFE
     YSNLQLPEVV DLGDNGERTF NVSVDVMNTG DKDGHEIVQL YVSDIECATL RPCKELKGFA
     KLWVPKGGKV KAIISLDKYA VSYWDEEEEK WLAEKGTFRV VISRSADPKD EVLQREFRLE
     RDLYWRGV
//