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Database: UniProt
Entry: H0EFE4_GLAL7
LinkDB: H0EFE4_GLAL7
Original site: H0EFE4_GLAL7 
ID   H0EFE4_GLAL7            Unreviewed;       839 AA.
AC   H0EFE4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   22-FEB-2023, entry version 41.
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=M7I_1217 {ECO:0000313|EMBL:EHL02702.1};
OS   Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHL02702.1, ECO:0000313|Proteomes:UP000005446};
RN   [1] {ECO:0000313|EMBL:EHL02702.1, ECO:0000313|Proteomes:UP000005446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX   PubMed=22302591; DOI=10.1128/EC.05302-11;
RA   Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT   "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT   of a species from the Helotiaceae family.";
RL   Eukaryot. Cell 11:250-250(2012).
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:EHL02702.1}.
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DR   EMBL; AGUE01000020; EHL02702.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0EFE4; -.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   InParanoid; H0EFE4; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000005446; 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:UP000005446};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..839
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003532388"
FT   DOMAIN          761..829
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   REGION          711..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   839 AA;  90224 MW;  3DEAED4AF2831D55 CRC64;
     MLWSSSLASI VVLAASASAQ LDGAQSPPSY PSPWMRGGNG WQDAYAKAQA FVSQLTLLEK
     VNLTTGVGWE GEACVGNTGS IPRLGFRGFC LQDSPLGIRF ADQASAFPSG MNVAATWTTR
     LFKSRGRAMG DEHRGKGIDV QLGPVAGPLG RVPAGGRNWE GFSPDPVLTG VAIGETIKGI
     QDGGVIANAK HYIMNEQEHN REPSGSFAAY SANVDDKTMH ETYLWPFADA VHAGVASIMC
     SYNQINNSYG SQNSYTLNYL LKNELDFQGF VVSDWWAQHT GVASALAGLD MTMAGDQGLA
     SGNTYWGGNL TAAAINGTLP QWRLDDMVTR IMAAYYKVGR DTARVDVNFN SWSSETYGYI
     HPQANEGYQQ INYHVNVQSD HAKLIREIGG ASTVMLKNVN NALPLKKPKS VAVIGEDAHD
     NPGGPNACGD RGCNTGTLAM GWGSGTANFP YLIAPVTALR AQAAKDRTLF ANVSNNYDLD
     AAAKAASNAS VAIVFANADS GEAYITVDGN SGDRNNLTLW GNGDALIKKV ASVNPNTIVV
     LHTVGAVIVE DLKNNPNVTA ILWAGLPGQE SGNAITDIIY GYRNPSAKSV FTWGKKREDW
     GVDVIYTPTS NPPQLNFNEG NFIDYRYFDA NNIEPSYEFG FGLSYTNYSY SNLQISKNDP
     GPYQPTVGMT KAAPTLGTID KDPAHAEFPT GFRAVFKYIY PYLTGPVLTN QPESWPAKSQ
     DGSPQPRVGA GGSAGGNRQL WDVMYTVSCT VTNTGGVKGT EIPQLYLSLG APTDPKIVLR
     GFDDLILDPG ESNTFTYKLT RRDISNWDPV TQNWVISPYP KTVYVGASSR DLKLKGVLP
//
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