ID M7TV45_BOTF1 Unreviewed; 827 AA.
AC M7TV45;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BcDW1_6150 {ECO:0000313|EMBL:EMR85155.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR85155.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB707917; EMR85155.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TV45; -.
DR STRING; 1290391.M7TV45; -.
DR HOGENOM; CLU_004542_2_1_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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:SF14; BETA-GLUCOSIDASE D-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:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..827
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004085973"
FT DOMAIN 740..809
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 454..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 86685 MW; 9A74D654137DCD78 CRC64;
MKGHQVLSVV SALSFFTSGL CASNSTTTST SSSGLLSDGN VNLGAASDAY EKAVTFISSL
TNAQKIAIIT GQSIDSDNVT WTPLASKDGA VGINMNFFVS GFSTPQAVSM TWNRTLFLEN
FSALGKEFYA IGASLADGPI SSPMGRVAYG GRNGEGFAAD PYLNGIAMGK AISGINSAGV
VTAGRHFLFN EQETNRSSTN RYSSNVDDKT TREVYLWPFA DAVKSGMMAA MCAMNKVNNT
LSCENSELLN NYLKTAIGFP GMVTPDQGAQ STSFGSANGG LDYGSSSLWS EEILEAGIAN
GSFTQERLDD MAVRNVIGYY FAGLDDGLIP SETGYTDYRD VREDHADVIR QVGGEALVLV
KNTQDGTGRG LPLSKPRTIS LFGAHAGPAM AGPNRAFSVQ GTPADTYQGH LAGPGGSGQP
SLSYLVTPFQ AISARAIADR SMIWWVLNNT YTDTSSSSGG MGGGMGGGFT GGGMPTTNDN
STSTTATTGT SPGNSSSSSN SSSSSGPGSS SGSTSSVNLG NLGSGTALSP SISNYALNSA
VCLVFINADS GEGADRSELS NDEQDTMVTT VADNCNNTIV VVNTVGPRIL DAWIEHENVT
AVLYSGLLGQ ESGNAIADVL YGDVNPSAKL GYTLPKNATD YPSEFDVCEE EQCDYTEGVY
LDYRYFDSKN ITVRYPFGYG LSYTNFTYST EVTATIVNQT ALTYKYASGQ LGLGGEADLW
DDVLNVTTSV SNSGTVAGAE VAQLYISFPD EAEQPIRILR GFEKVNIAPG ESADIAFSLR
RRDISYWDAT AQAWAIASGD YTITVGASSR DLKASTKLTL TIGSTST
//
