ID   A0A3M2SH51_9HYPO        Unreviewed;       841 AA.
AC   A0A3M2SH51;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   22-FEB-2023, entry version 13.
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=CDV36_003467 {ECO:0000313|EMBL:RMJ16868.1};
OS   Fusarium kuroshium.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ16868.1, ECO:0000313|Proteomes:UP000277212};
RN   [1] {ECO:0000313|EMBL:RMJ16868.1, ECO:0000313|Proteomes:UP000277212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ16868.1};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) 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:RMJ16868.1}.
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DR   EMBL; NKUJ01000041; RMJ16868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2SH51; -.
DR   STRING; 2010991.A0A3M2SH51; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000277212; 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:SF13; BETA-GLUCOSIDASE K-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   SMART; SM00758; PA14; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277212}.
FT   DOMAIN          408..567
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   841 AA;  92285 MW;  60F66B436BE9A74E CRC64;
     MVLKVQAASE VSKDFDVEHV IKNASVSEKI TLLSGQDFWH TAPLPRFNVP SIRVSDGPNG
     VRGTKFIDGV PAACLPCGTG LAATWDHNLL YQAGILIGNE CKAKGAHCWL GPTVCIQRSP
     LGGRGFESMA EDPYATGKLA AAYIKGVQST GVVSVIKHWL ANDQEHERVG VNVVVSERAL
     REIHMLPFQI ALRDAAPGAV MSCYNKVNGK HVSESRELLD GLLREEWQWK GLIMSDWFGT
     YSTAEALNAG LDLEMPGPTR QRGQLLDLAV STRKVSRTTI DTRARNVLEF VQRCNKVVVA
     SEEGGRDFPE DRQLNRQLAG DSVVLLKNEG GLLPLKHPFK SIALIGPNMK NTSFCGGGSA
     HLQPYYTVSP FDGIVDQLPP DVEVKYEIGA SASGWNPLLQ ASDVMTPDGS PGLRIRFYRE
     PPTVPDREVI DESLLPESSW QLMGYSHPKL EKLFYAKVEG DFIGQATGPF EFGLAVYGSA
     RFYVDGQLLI DNSAVQRGGT FFFGKGTLEE KAKMHIIQGQ KYRIKVEYES APSSKLVKPG
     VVNFGGGAGR LGLVRVIDPD ASIRAAVDAA TQSDVSILCV GLTRDQESEG FDRQHMELPG
     FLPRLISAVL DAAPDTIIVS QSGTPFNMLP WAERTKTHLH AWMGGNETGN GIADVIFGKI
     CPSGKLPLSF PRRIEDTPTY LNFGSERGRV IYGEDIYVGY RYYEKVDRDV LYPFGHGLSY
     TTFTYSNLTI TSLHVTLEVT NSGAVAGAEA AQLYIAADPT TSSIAKPKKE LKGFKKVHLQ
     PGETQRVQIP LDRFTTAFWD EEMHCWVCEK GVYKVLVGSS SQKILLEGKL EVMETTYWSD
     L
//