ID A0A1L7WBM1_9HELO Unreviewed; 797 AA.
AC A0A1L7WBM1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=PAC_00046 {ECO:0000313|EMBL:CZR50174.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR50174.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR50174.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR50174.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FJOG01000001; CZR50174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7WBM1; -.
DR STRING; 576137.A0A1L7WBM1; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000184330; 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:UP000184330};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..797
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012069409"
FT DOMAIN 713..785
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 797 AA; 84935 MW; 2CEC7923D453248A CRC64;
MVIMTIRGPP LLVSLLFGIV MAADTHFTSP EVLPSPETQG VGWTDAYNKA DNLVSKLTIE
QKVSLVTGYY GASGCNGNIA PIPSLGFGGL CLQDGPVGIR LADLASTFPA GLTAAATWDK
DLIYDRGKAI GSEFRGKGAN VILGPVGGPL GRHLLGGRNW EGFSPDPYLT GVAMASSIKG
IQDAGIQATA KHFIGNEQET MRGGSLTANG TLVDAISSNI DDRTMHELYL WPFADAVKSG
VSSVMCSYNR VNQTYSCENS KILNGLLKGE LGFQGYVVSD WSATHSGVKA ITSGLDMNMP
GPISDADPTS NNTYFGQNIT LAVNNGSLPE DRLDDMARRV LTPYFFLGQD ATDFPTVDPS
TIYVLLQTYG YSATSLGLPP APASRDVRQD HKKLIREMGA AGVVLLKNTN GTLPLRSQTN
IGVFGNSAGD VTDGLYYEGT KASGTGFGFQ QGTLSVGGGS GTGRSTYIIS PLQTLLERSD
ARVQYILDNE FIASGDLSSI YPTPDACLVF LKTWASEGYD RTSFENDWDS TVVVNNITAK
CPNTVVITHS GGVNTMPWAS NPNVTAILAA HYPGQESGNS IVDVLYGDVN PSGRLPYTIP
AKESDYDIPV VNVTGPEALD SSAWQSDFAE GLFIDYRHFD AKNITPLFEF GFGLSYTTYG
INEPPSVKSV NNISSPFPLP STTVAPGGNP DLYTELFNVK ANVSNTGAVP GAAVLQLYVS
LKDAAVPEGT PVRVLRGFEK VHIEPGDSAA VEFQLTRRDL SFWNTTAQDW QIPAGDALLS
LGFSSRDLRS SSKVRLL
//
