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Database: UniProt
Entry: A0A093YQB2_9PEZI
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ID   A0A093YQB2_9PEZI        Unreviewed;       814 AA.
AC   A0A093YQB2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 32.
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=V492_07503 {ECO:0000313|EMBL:KFY07039.1};
OS   Pseudogymnoascus sp. VKM F-4246.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY07039.1, ECO:0000313|Proteomes:UP000029299};
RN   [1] {ECO:0000313|EMBL:KFY07039.1, ECO:0000313|Proteomes:UP000029299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY07039.1,
RC   ECO:0000313|Proteomes:UP000029299};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY07039.1}.
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DR   EMBL; JPJU01002657; KFY07039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093YQB2; -.
DR   STRING; 1420902.A0A093YQB2; -.
DR   HOGENOM; CLU_004542_2_1_1; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000029299; 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; 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:SF5; BETA-GLUCOSIDASE M-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 2.
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   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:UP000029299};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..814
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001889628"
FT   DOMAIN          736..802
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          208..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   814 AA;  87274 MW;  EFAAD08D164EF25B CRC64;
     MVSFTTKLAT ASCLSLSVFA GAASGQNITD DTHFYGQSPS VLPSPETPGT LSWQTAHAKA
     VALVSQMTLA ERANITVGYE PTTGCSGATG SVPRLGWEGL CLADAGQGLR ATDFVNAYPA
     GISVGTSWNK ALTLQRATHM AAEFKRKGVH VILGPVVGPL GRVALGGRNW EGFSNDPYLS
     GSLVHDTIEG IQNAGVIASV KHFIGNEQEN NRNPIEPGTT GGGIGGGGGL SSGGPSNNLS
     QTIESLSSNI DDKTMHELYL WPFADAIHAG SASVMCSYQR INNTYGCHNQ KTQNGLLKTE
     LGFEGFVVSD WGAQHAGIAS AEGGLDMAMP DGGEFWGVDG SNLTTFVKNG SMPEARLTDM
     ATRIVAAWYQ LGQDRDFPPV SLPIQYNVSH KAVNARDPAS KPILLQGAIE GHVLVKNVNK
     TLPFKKPKLL SLFGYDAVAP PRVNLVDPNF NFKFGFLSNS EFFWKDAFVS PFVNPGQIGP
     NGTLIVGGGS GGTAPAYISA PFDALQERAY TDNFQLLWDF HSTAPQVDQA SDACLVFINA
     FATEGIDREG LHDDYSDDII LNVASACSNT VVVIHNAGVR LVDTWIDHPN ITAVMFAHLP
     GQDSGRAAVS LLFGDESPSG KMTYTVAKNE SDYNVPLARA TDEFFFFPQD DFTEGVYIDY
     RDFDRKNITP RYEFGFGLTY TTFEYSDLSV SLVQNASTSR DAPESPIIEG GKESLWDVIA
     TASAVVTNTG DVTAKEVAQL YVHIPGGPVR QLRGFDKVEI APGESATVRF TLLRRDLSDW
     NVAEQAWVLQ QGEYSVWVGA SSRNLPLTGE LTIS
//
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