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Database: UniProt
Entry: H0EY78_GLAL7
LinkDB: H0EY78_GLAL7
Original site: H0EY78_GLAL7 
ID   H0EY78_GLAL7            Unreviewed;       670 AA.
AC   H0EY78;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Probable beta-glucosidase G {ECO:0000256|ARBA:ARBA00039579};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE   AltName: Full=Beta-D-glucoside glucohydrolase G {ECO:0000256|ARBA:ARBA00041276};
DE   AltName: Full=Cellobiase G {ECO:0000256|ARBA:ARBA00041601};
DE   AltName: Full=Gentiobiase G {ECO:0000256|ARBA:ARBA00041808};
GN   ORFNames=M7I_7776 {ECO:0000313|EMBL:EHK96514.1};
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:EHK96514.1, ECO:0000313|Proteomes:UP000005446};
RN   [1] {ECO:0000313|EMBL:EHK96514.1, 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   -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC       involved in the degradation of cellulosic biomass. Catalyzes the last
CC       step releasing glucose from the inhibitory cellobiose.
CC       {ECO:0000256|ARBA:ARBA00024983}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:EHK96514.1}.
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DR   EMBL; AGUE01000242; EHK96514.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0EY78; -.
DR   HOGENOM; CLU_004542_2_3_1; -.
DR   InParanoid; H0EY78; -.
DR   Proteomes; UP000005446; 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:SF19; BETA-GLUCOSIDASE G-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   Reference proteome {ECO:0000313|Proteomes:UP000005446}.
FT   DOMAIN          585..656
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   670 AA;  72519 MW;  2D98F682413AF954 CRC64;
     MYERGLYMGE EFRGKGAQVA LSPVAGPLGR SAYAGRNWEG FSPDPYLTGK AMEETIKGIQ
     AAGVQATAKH WIANEQETQR NPTYNGSVIV QESISSNLDD RTMHELYMWP FANAVRAGVS
     SVMCSYQRLN GSYTCENSKA LNGLLKEELG FQGYVMSDWG GTHSGVPSIE SGLDMNMPGG
     LGLYGLTFGE ASDFGRNVSI AVSNGTLDAS RVDDMIIRIM TPYFHLGQDV DFPLVDPSSG
     DLNTFSPTDT WFRYFNLNGT RSRDVRGNHS ESIRELGASA TVMLKNVNNT LPLKAPKVIA
     IFGNDAGEPA PGYLNQNNYE AGTLVAGGGS GTGRLTSLVT PLDALKAQAL KTGAIIEPYL
     NNTLIADTDI QTLLNPGQPD VCLVFLKTWA EEAADRKSLD TDWRGNDVVE SVASYCSNTV
     VITHSSGINN LPFANHTNVT AILAAHFPGE QTGNSIVDVL YGAVNPSGKL PYTIALEIDD
     YNALPLTSVN STDPYAWNIY FEEKLEIDYR YFDAQNMSVR YEFGFGLSYT TFSVSDLTFL
     KCGNATVTSV APAGAVNPGG NEALWETLWY VTVELTNTGT VAGAEVPQLY LSLPASAPAG
     TPPKQLRGFE KVYLEPGASS TVTFPLMRRD LSYWDIISQD WLIPEGEFGF SVGFSSRDIK
     LTAGLTVVDS
//
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