ID A0A4Y9Z0E6_9APHY Unreviewed; 937 AA.
AC A0A4Y9Z0E6;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=EVJ58_g1194 {ECO:0000313|EMBL:TFY68115.1};
OS Rhodofomes roseus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Rhodofomes.
OX NCBI_TaxID=34475 {ECO:0000313|EMBL:TFY68115.1, ECO:0000313|Proteomes:UP000298390};
RN [1] {ECO:0000313|EMBL:TFY68115.1, ECO:0000313|Proteomes:UP000298390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105464 {ECO:0000313|EMBL:TFY68115.1,
RC ECO:0000313|Proteomes:UP000298390};
RA Buettner E., Kellner H.;
RT "Genome sequencing of the rare red list fungi Fomitopsis rosea.";
RL Submitted (JAN-2019) 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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:TFY68115.1}.
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DR EMBL; SEKV01000037; TFY68115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y9Z0E6; -.
DR STRING; 34475.A0A4Y9Z0E6; -.
DR Proteomes; UP000298390; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000298390};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..937
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021506260"
FT DOMAIN 857..926
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 937 AA; 99027 MW; 5D9006EA4C62072E CRC64;
MAVLLSARLA ALAAFLVVAV SGQSPVAISS AVASSAIASS AAASSAAASS VAISSVAVSS
AAAASSAASS AAVSSAASSA AASSAVSSAA ATSVVSSAAA ASSSGDVGEV SGVSYTVQDT
YTIYGIPAPT DPASVATSPT AGGEPPYWTG LGTEVGWQTL SVSSYAFTSY PIASSTPVPP
VFPALSPLYP PAVDNAGPQI IPDFSAAWDA AFARAQAFVS TLTLEQKVNV STGIGWEKGL
CVGNIGQVGD WPGLCLEDSP LGIRYTDFNT VFPAGISTAA TWNRTAIRIR GQQMGEEFRG
KGAHVQLGPM MNMGRVAQGG RNWEGFGTDA FLSGEAAYET TLGIQSAGVQ ACAKHYIDYE
QEYKRTQESS NVDDRTNHEI YLKPFLRAVM AGTASVMCSY NMINDTYACE NDRTLNQLLK
SELGFRGYIM SDWGGQMSTL SAMAGLDMSM PGDITLGSGN SYWGPNLTAF VENSTIPLSR
VDDMATRILT SYYLLGQDEN YPNVSFNAFN PYDTEHNLNV DVQADHYQIV REIGAQGAVL
LKNTNNALPL NAPRSLLVVG SDAGNNPMGP NGCTDRGCDE GVLGIGWGSG SANFPYLISP
YDVLQEQARI DGTSISNWYL DWNTDGVAAI ANLSDVALVF VNSDSGEGYI TVDGNLGDRN
NLSLWHNADN LINAVASQNP NTIVIAHSVG PSIIEPWVEN PNVTAIVWAG VPGQEAGNSI
VDVLYGAYNP SGRLPYTIAK RAEDYGVFLV LGGEGDTLLS IPYDEGLFYD YRRFDQYNIT
PRYEFGFGLS YTTFEYSNLA LGIVPQYDPT SWDLEAAWAE GAPTPQGEGS STALWLHRPF
LSVEFDLENT GALAGTEIPQ VYVHFPAGSG EPPSLLKGFD TVYLEPGELQ SVYITISRYE
LSIWNVEAQG WQKPSGTFTL SVGASSRDFR LNDAIPI
//
