ID A0A1S8B527_9PEZI Unreviewed; 904 AA.
AC A0A1S8B527;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=BK809_0006796 {ECO:0000313|EMBL:OMP82486.1};
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:OMP82486.1, ECO:0000313|Proteomes:UP000190776};
RN [1] {ECO:0000313|EMBL:OMP82486.1, ECO:0000313|Proteomes:UP000190776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F98.1 {ECO:0000313|EMBL:OMP82486.1,
RC ECO:0000313|Proteomes:UP000190776};
RA Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT in grapevine trunk diseases.";
RL Submitted (JAN-2017) 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 ECO:0000256|RuleBase:RU361161};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:OMP82486.1}.
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DR EMBL; MSZU01000114; OMP82486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8B527; -.
DR STRING; 420778.A0A1S8B527; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000190776; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
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; IPR019800; Glyco_hydro_3_AS.
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:SF10; BETA-GLUCOSIDASE F-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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000190776};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..904
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012074423"
FT DOMAIN 807..881
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 702..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 96788 MW; CD70DAF79EFDFE0A CRC64;
MSVSLLIGAA SAQPLVLASL LSLPFFPSRA SAQSLPSDPR YDYFLSIFQA ANQTVSTNAA
VPDGYVAAPW YPTPYGGWTE DWSTSYAKAA ELVSNMTLAE KTNITVGTGY FMGRCVGNTG
SAPRLGFPQL CLQDSALGVK GTENNTAFTP GITVGATWNK DLMYARGEAI GEEFRGKGVN
VHLGPTVGPL GRKPRGGRNW EGFGADPVLQ AVGGAQTIKG VQAQGVMATI KHLIGNEQES
YRMYNPFQPG ISANIDDRTM HEIYLWPFAE GVRAGVVSVM GAYNAVNGSA STQNSYLINN
LLKDELGFQG FIMSDWFAQI SGAGAALAGL DMSMPGDPTI PLFGNSWWAF HLTEAVLNGS
VPVDRLNDMA TRIVAAWYQV GQDQDYPDIN FSTWTEDAEG LLYPGALISP TRVVNEFVDV
QDDHAAVVRN ISTEAVTMLK NDNGTLPLKE STPLKVFGTA AEKNPDGINS CSDKACNKGT
LGMGWGSGTA DFPYLDSPMD ALNSRADNVT FYNTDSFPSD AVVNDGDVAL VFVTSDSGEN
YLSVEGNPGD RTSSGLNVWH NGDELVQKAA EKYDNVIVIV QTVGPILVEE WIDLPSVKAV
LFQHLPGQEA GESLTTVLYG DESPSGHLPY SIVKKEDDLP DSVGIVGFEL GQPQDTFSEG
LYIDYRYLNK QKIAPRYPFG HGLSYTSFNY SATIAAGVEL TSTPPTRPAK GSTPSYSTEI
PQPSEAVAPE GFDKVWRYLY SWLSESEANS AYEKRNSSDY PYPEGYSTEQ KAGVPAGGAQ
GGNPALWDAA FNVSVTVANT GSAPGKAVAQ LYVQYPEGSS YDTPVIQLRD FGKTATLQPG
ESETLALTLT RKDVSVWDVV SQNWVVPDVD GEYKFWVGES SGALGVACSS TGLTCEGGQE
SPVA
//
