ID A0A1B8FU08_9PEZI Unreviewed; 735 AA.
AC A0A1B8FU08;
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=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=VE02_05029 {ECO:0000313|EMBL:OBT87077.1};
OS Pseudogymnoascus sp. 03VT05.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT87077.1};
RN [1] {ECO:0000313|EMBL:OBT87077.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03VT05 {ECO:0000313|EMBL:OBT87077.1};
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 -!- 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; KV459409; OBT87077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8FU08; -.
DR Proteomes; UP000091872; Unassembled WGS sequence.
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:SF29; BETA-GLUCOSIDASE L-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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..735
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008608039"
FT DOMAIN 656..726
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 735 AA; 77080 MW; 6185E46150157099 CRC64;
MAFLKSATLA LAALLPLTSA VPTARADDGG WDAAHAKAVT ALAKLSLGDK VKMVTGEGWE
KGPCVGTTAE ISSIGYPQLC LQDGPLGIRF AQGITAFPAG VQAASTWDIA LIKARGNALG
TESKAMGVHV QLGPVGGPLG KIPHGGRNWE GFSPDPYLTG VAMAETITGM QNAGVQACAK
HYIGNEQELN RDTMSSTIAD RVNHELYLWP FADSVKANVA AVMCSYNRLN GTYACESDLA
LNGLLKGELD FRGYVVSDWN AQHTTVGSAK AGMDMSMPGD NFGDNNYLWG TALTNAVSGG
QVDESRVDDM VERILASWYY LGQDAGYPKV GWSSWNGGVG GPEVQGEHKI VARDIARDGI
VLLKNENNAL PLKKPASLAI IGNDAINNPN GPNACVDRGC DVGTLAMGWG SGAAEFPYLI
SPLDAIQKQA TADGTTIVSS TTDSTSEGAA AAGKADTALV FINADSGEGY ITVEGQAGDR
ADLDPWHNGN GLVEAVANVN KNTIVVIHSV GPLILEKILA LPNVVAVVWA GLPGQESGNG
LVDILYGSKS PSGKLPYTIA KQASDYGTSV RSGDDDFSEG LYIDYRHFDQ AGIEPRYEFG
FGLSYTTFGY SDLTTTYTDK TEGSTTTAPG GAEGLYDTVV TVTAKITNSG TVEGAEVAQL
YIGLPSTAPP TPVRQLRGFS KINLAAGESG TVTFNLRRKD LSYWDTDAQK WVTPTGDFTV
SVGASSRNLA LKGTM
//