ID A0A010SI09_9PEZI Unreviewed; 765 AA.
AC A0A010SI09;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 22-FEB-2023, entry version 35.
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=CFIO01_02723 {ECO:0000313|EMBL:EXF84408.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF84408.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF84408.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF84408.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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:EXF84408.1}.
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DR EMBL; JARH01000168; EXF84408.1; -; Genomic_DNA.
DR RefSeq; XP_007591916.1; XM_007591854.1.
DR AlphaFoldDB; A0A010SI09; -.
DR STRING; 1445577.A0A010SI09; -.
DR KEGG; cfj:CFIO01_02723; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_1_1; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000020467; 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:SF5; BETA-GLUCOSIDASE M-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:UP000020467};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..765
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001456569"
FT DOMAIN 686..754
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 765 AA; 81624 MW; 855F198770C4CAF1 CRC64;
MVNNLISTLA AALAGLTLCA AQDSYTNETD PYYGQSPAVY PTPVGNGTTN EKWATAYQRA
KSLAAQMTVE ELANFTHGWD GLCTGNTGSV PRLGIEPICL QDGPDGVRAQ EFVSAFPSGI
HLGATWDKNL SYAYGEALGA EFRGKGINVG LGPVGGPLGR IARGGRNWEG LSNDPYLSSV
GVGGITKGMQ DAGTIACPKH WILNEQEYRR NPSVEEGEAG SSNVDDRTLH ELYVFPFMDA
LKEGAASVMC SYNRANNSYG CQNSKLLNGV LKTELGFEGF VVSDWGAQHA GVATANAGLD
LVMPNEAFWG ASLVEAVNNG SVTRERIEDM TTRILAAWYY IGQDSDDYPA VGAYSNLQKH
APVDVQNGHK AIIREIGAAG TVLVKNVNGT LPFKNPKFLT VYGYDASLPP SPWGSTSYGP
SWGTVLADTF NGTLLSGGGS GTTTPPYVIT PFQAIQDRVI EDGGVVKWDF YSENPQPNYV
NSEACLVFIN AWASEGYDRP SLTDEFSDNL VNNVAANCSN TVVVLHSAGT RVVEAWADHP
NVTAILFAGL PGQESGNSLV DILYGDVNPS GRLPYTVARA ESDYGNLLNS TVEAGPFPQD
DFTEGLFIDY RAFDRDGISP RYEFGFGLSY TTFGYSSLSA SPASGVSAGV PDPSIAIVQG
GHPALWEEVV SVSVTVQNTG GVGGHEVAQL YVGIPVEGTP AKQLRGFERV YIEAGGSATV
EFALTRRDLS FWDVSAQQWR LSEGEYGVWV GASSRDLRVN GTFTI
//
