ID A0A0P7BTK9_9HYPO Unreviewed; 886 AA.
AC A0A0P7BTK9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN ORFNames=AK830_g2840 {ECO:0000313|EMBL:KPM43667.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM43667.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM43667.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM43667.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-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 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:KPM43667.1}.
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DR EMBL; LKCW01000029; KPM43667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BTK9; -.
DR STRING; 78410.A0A0P7BTK9; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
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:SF12; BETA-GLUCOSIDASE A-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 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:UP000050424};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..886
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006136198"
FT DOMAIN 807..876
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 744..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 95960 MW; 27B23C5AD30EF123 CRC64;
MQPTPALPLL SLALVSLARS HADTQVPLQV DAREDTLAFS PPHYPSPWMD PAAPGWEDAY
ARAKEFVSQL TLPEKVNLTT GVGWMSERCV GNVGSIPRLG MRGLCMQDGP LGIRLSDYNS
AFPGGITAGA SWSRKLWRER GLLMGTEANE KGIDVLLGPV AGPLGRAPTG GRNWEGFSVD
PYMSGIALAE TSLGIQEGGV VACAKHFVGN EQEHFRQSPE ARGYGYNITE SMSSNIDDKT
LHELYVWPFA DAVKAGVGSI MCSYQQLNNS YACQNSKLIN GILKEELGFQ GFVMSDWQAQ
HAGAATAAAG LDMTMPGDTS FNTGLSFWGA NLTLAVVNGT VPEWRIDDMA MRIMASFFKV
GRTVDDMPDI NFSSWSRDTF GYVQMAAKEN WEQINFGVDV VGDHGLHIRE AAAKGSVLLK
NSGSLPLKKP KFVAVIGEDA GGNPAGPNGC NDRGCDNGTL AMSWGSGTSQ FPYLIAPDQA
LQFQAHADGS RYESILNNNQ WAQTLQVISQ PNVTAIVFAN ANAGEGYINV DGNEGDRKNL
TLWKEGDDLI KNVSSVCPNT IVVLHTVGPV ILTEWYDNPN ITAIVWAGLP GQESGNAVAD
ILYGKTSPGR SPFTWGRTRE SYGTDLLYKP NNGQGAPQQD FAEGVFIDYR HFDRRSPSTT
GKASNSSNAP LYEFGYGLSW TTFEYSNLEV QAHIDTPYEP TSGETIAAPE LGNFSTDLSD
YTFPSNIRYI YQFIYPWLNT SSSGREASAD PEYGQTAEQF LPPNANNGSP QPKSPASGAP
GGNPQLWDVL YTVSATITNT GNATSDEIPQ LYVSLGGEGE PVRVLRGFER LEGIAPGQSF
IFTADITRRD LSNWDVVSQD WVITEHEKKV YVGSSSRNLP LTAVLN
//
