ID A0A4V1X8Y7_9PEZI Unreviewed; 836 AA.
AC A0A4V1X8Y7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 22-FEB-2023, entry version 11.
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=DL764_009514 {ECO:0000313|EMBL:RYO83056.1};
OS Monosporascus ibericus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX NCBI_TaxID=155417 {ECO:0000313|EMBL:RYO83056.1, ECO:0000313|Proteomes:UP000293360};
RN [1] {ECO:0000313|EMBL:RYO83056.1, ECO:0000313|Proteomes:UP000293360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110550 {ECO:0000313|EMBL:RYO83056.1,
RC ECO:0000313|Proteomes:UP000293360};
RA Robinson A.J., Natvig D.O.;
RT "Complete Genomes of Monosporascus.";
RL Submitted (JUN-2018) 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:RYO83056.1}.
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DR EMBL; QJNU01000915; RYO83056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V1X8Y7; -.
DR STRING; 155417.A0A4V1X8Y7; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000293360; 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:SF12; BETA-GLUCOSIDASE A-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:UP000293360};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..836
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020266398"
FT DOMAIN 758..826
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 710..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 90968 MW; FBE9761B8B2DB436 CRC64;
MHVTALLALW AAGSSAAGIQ PLASRETEER HDWAFSPPHY PSPWMNPTAV GWEVAYAKAK
AFVSQLTLME KVNLTTGVGT AQYLALDFAA YADGPLGIRF GDYSSAFPSG QTVAATFDRQ
LLYQRGRAMG AEAKGKGVSV LLGPVAGPIG RMPTGGRNWE GFSPDPYLTG VGMAETIKGI
QDEGVIACAK HFIANEQEHF RQVGEANGYG YNITETLSSN IDDKTMHELY LWPFVDATMN
GLLKGELGFQ GFVLSDWQAQ HGGVSTALAG LDMSMPGDTR FNTGFSFWGT NLTVAVLNGT
VPQYRVDDMA MRIMAAYFKV GMTLDQPPIN MNSWTKDTFG YRHFYAQEGY ERVNWHIDVQ
DDHGDLIREI GAKATVLLKN EGALPLKKPR FLAVIGEDAA PNPLGPNGCP DRGCNEGTLA
QSWGSGTADF PYLVSPYEAL ALQARQDHTR FEAVLDNYAT SQIESLVSQE DVTAVVFVNA
NSGEGYISVD GNEGDRNNLT LWGSGDELIK NVSSLCSNTI VVIHSVGPTL VTDWYDSPNV
TAILWAGVPG QESGNSITDV LYGRVNPAGR TPFSWAAKRE DYGADVMYEP NNDIPQQDFT
EGVHIDYRYI DSNNITPIFE YGFGLSYTTF SYSDIRVEKI AAPAYEPTTG QTNPAPTFGN
FSTDLSDYQF PDSLIRRIPG YIYPYLNVTD AEAATADPYY GLAPEEWLPP HAAEDAPQPL
HPAGPDASQQ PGGNAGLFDD LYTVTARITN TGNVVGDEVP QLYVSLGGPE DPPRVLRGFD
RLNVAPGQTV VFAATLTRRD LSNWDTAYQD WVVTEHPKTV YVGPSSRKLP LSATLA
//
