ID A0A2B7YIT6_9EURO Unreviewed; 726 AA.
AC A0A2B7YIT6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=AJ80_03405 {ECO:0000313|EMBL:PGH20778.1};
OS Polytolypa hystricis UAMH7299.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH20778.1, ECO:0000313|Proteomes:UP000224634};
RN [1] {ECO:0000313|EMBL:PGH20778.1, ECO:0000313|Proteomes:UP000224634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH20778.1,
RC ECO:0000313|Proteomes:UP000224634};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:PGH20778.1}.
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DR EMBL; PDNA01000038; PGH20778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7YIT6; -.
DR STRING; 1447883.A0A2B7YIT6; -.
DR OrthoDB; 2783936at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000224634; 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:SF29; BETA-GLUCOSIDASE L-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 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:UP000224634};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..726
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012835175"
FT DOMAIN 646..716
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 726 AA; 77118 MW; 61DEC6BBDBF0F7F5 CRC64;
MQYSLILAAL SAASVTAQKG DWAASAAKAS QSLQGLSLQQ KAGIVTGTGW MQGPCVGNTG
EAQSIGFRSL CLQDGPLGVR YAGSVTAFPP AIQAASTWDV ELIKQRAVGM GEEARALGVN
VLLGPSAGPL GKIPQGGRNW EGFGADPYLQ GVGMYETIVG IQESGVQACA KHYIGNEQEY
RRSELSANID DRTVHEMYLW PFADSVRANV ASVMCSYNKL DSVYACENDE YLNQILKTEL
DFPGFVLSDW GAQHTTDGSA KGGLDMTMPG DNFGDNQFLW GNNLVNAVNS GQVQQSRVDD
MVSRILTSWY YTGQDSGFPN VGFNSWNGNG GPNVQGNHKE VARAVARDGI VLLKNTNNAL
PLNKPESIAI IGSHAFDNPQ GPNACVDRGC NTGPLGMGWG SGTVDYPYLI APYDAIKQQA
DADGTRVTQA DSDNFSHGGT AARAAETAIV FITADSGEEY ITVEGNAGDR NNLNAWHTGN
ELVAAVAEGN QNTIVVVHSV GQILLESFIE LDNVVAVVWA GLPGQESGNA LVDVLYGKTA
PSGKLPYTIG KRAEDHGVSI VRGDDNFSEG LFVDYRHYDK QGIEPRFEFG FGLSYTTFDY
SGLTATYSDK SPADNVAAPG GSASLYETVA TVTATITNSG DVAAAEVAQL YLGLPSSAPE
TPAKQLRGFQ KVHLEPGQSA TVQFPLRRKD LSYWDAQGKN WVIPSGAFAV HVGASSRDIR
LTGSMA
//
