ID A0A1B8G4P4_9PEZI Unreviewed; 800 AA.
AC A0A1B8G4P4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=VE02_00593 {ECO:0000313|EMBL:OBT90710.1};
OS Pseudogymnoascus sp. 03VT05.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT90710.1};
RN [1] {ECO:0000313|EMBL:OBT90710.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03VT05 {ECO:0000313|EMBL:OBT90710.1};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
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}.
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; KV459354; OBT90710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8G4P4; -.
DR Proteomes; UP000091872; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..800
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008608189"
FT DOMAIN 716..788
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 800 AA; 85620 MW; 3AADC49EBE243883 CRC64;
MAYLHLGKLL TTLISFFLVA SAQSSWDHEL FTSSPPVYPS PSTDGNGWES AYAKARIFAA
NLTLDEKAGL LTGNIRGPCV GNLVPIARLG FKGLCMQDGP AALRQATFVS VFPAGLTIGA
TWDRKLMNTR GSYLGAEFKA KGAHVMLGPV AGPLGRSAFA GRGWEGFSPD PYLAGVAMEE
TITGIQSTGV QANAKHWIGN EQETQRVPSN NGGVKIDAVS SNIDDRTMHE VYMWPFANAL
HAGVASVMCA YNRLNASYAC QNSKILNGLL KEELGFQGYV VSDWGGTHSG VASVKAGLDM
DMPGSINFQS PGPSYFGGNL TIGVNNGSLT MDRIDDMVHR VMTPYYFLKQ DASYPSIDQS
SAPLNKWGIH PYLQSFVYGA KVNVDARGTH AKLIREAAAA GTVLLKNVGN ILPLKSPKNI
GVFGNDAGDN INGVYTLNVI RDKGYEYGTL TIGGGSGTGR PTYVVTPMDA IKARAAADGS
IVQFILNNSY LASDPNLAFS TFAPSPPDVC LVFLKTWATE GSDRTTLEAD WNSAAVVQNV
ADRCSNTVVI THSGGPNTMP WASHQNVKAI VAAHFPGQES GNSIVDILYG VVNPSGKLPY
TIANSEAEDK FAPITDSPEL RATTDPNAWQ SDFEEGPLID YRHFDYYNSS VLYEFGFGLS
YTTFGMANLV IAKIDEKVTA RAPAAKTAPG GNPNLFKTIF RITVAVSNTG ALAGAAVPQL
YLSLPPVDGI TASALRVLRG FEKVLLQPGE SQTVTFNLMR RDVSFWDTVS QEWVISPGKI
GVHAGFSSRD FKAESSFTPL
//
