ID A0A0G2GN89_9PEZI Unreviewed; 801 AA.
AC A0A0G2GN89;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=UCDDS831_g06102 {ECO:0000313|EMBL:KKY18310.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY18310.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY18310.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY18310.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY18310.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY18310.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) 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 -!- 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:KKY18310.1}.
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DR EMBL; LAQI01000133; KKY18310.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2GN89; -.
DR Proteomes; UP000034182; 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:SF14; BETA-GLUCOSIDASE D-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 2.
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..801
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002544566"
FT DOMAIN 713..779
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 184..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 85013 MW; 11858C616D35E3F2 CRC64;
MRSSLSILSA VTLLVQGLHA YSTNFTSQNL ASGTIKLGDW QNAYDRAKTF VDGLSTSEKI
SLITGSDVSN FTALYFRDSG DSILDYFYVT TWPLSSAVAM TWDKDQMYTM YKALGDEFYA
KGINVANGPV SQPLGRSPWG GRNGESFGPD SYLNGIAFGL SVKGYGDAGV ISGAKHFLLN
EQENNRTQSS GGGGGGGSPP SDGGNSTMPS GGDNSTSSDG GMGGGMGGSD SSSESTAYSA
QVDDKTLHET YMWPFYDGVK AGLGAVMCAL NRVNETYACE NQDLIGGMLK TEIGFPGFVF
GDVGGQKTAF GSANAGMDYG SSSTWSNSTI NTGLNNGSLT EARLTDMAVR NVLPSYYFNQ
QDGTYPATAG LEDYVDPRAN HSKIARNIAA SSLVLLKNTN GALPLNKPRT MSIFGAHAGA
ANAGPNDPLS VTGSDDVYQG HAASLGGSGT GSFAYLITPH YALTTKVLED GTMFRWLMND
TAYASSSSGM GGGVSGYSSG TGAAHTYAGY AADTDVCLVF LNAYSGEGAD RGELYNTDQD
AMVTSVASSC NNTIVVINAI AARLVDAWID NDNVTAVVYG GMLGQESGRA IVDVLYGDVN
PSGKLTYTLA RNESDYNTPL CTDLVCDFAE GNYIDYKYFD AYNVTPRYEF GFGLSYTTFQ
YAADLTVAKS PNAGLDQKYS QGARAVGGRE DLWDVVATAE TEVSNTGARD GAEAVQLYVA
FPAAAGQPVR QLRGFEKVHL AKGEKKAVKF ELRRRDLSYW DVEAQNWAVA SDLDLQAHAI
PKVRMERTIG WDISNSMQEL K
//
