ID A0A0F4GKS5_9PEZI Unreviewed; 864 AA.
AC A0A0F4GKS5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
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=TI39_contig473g00008 {ECO:0000313|EMBL:KJX97682.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX97682.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX97682.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX97682.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-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:KJX97682.1}.
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DR EMBL; LAFY01000465; KJX97682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GKS5; -.
DR STRING; 1047168.A0A0F4GKS5; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000033647; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000033647};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..864
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002468791"
FT DOMAIN 785..852
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 864 AA; 92561 MW; 8E0C50B09E9833E2 CRC64;
MRAAPWLAAA SYITLSCAQD ATNATIPPDP IEKVLKSLKL IPDGLVGIAA VILAAKANDA
HDQIVGTLKN QTLSDPRKLT DPEAYYSYGQ SPAVYPSPQG TGPANWSTAY AIARSLVSQM
TIEEKVNLTI PASDFAGCSG FSGSVPRLGF PGVCLNDGPS GVRVANTNHT SGFPAQIAIG
ASWNRTLSYW RSKQMGVEYR AKGVNVALGP VVGPLGRVAK GGRNWEGFTN DAYLAGQLVG
PAVEGLQESV VACVKHFIGN EQETQRNPFM AGYLAVAGIN LNNSVSANID DQTMHELYLW
PFYDAVRAGV GSVMASYNRV NNSYASQNSK LLNGLLKTEL GFQGFVVSDW GGQHTGVASA
NAGLDMVMPY GIWWGNGQLE QAANNGSVDA SRLDDMATRI VASTSRFANI TIPGIAANND
TDPSSELTTQ VLLEAAIEGH VLVKNVNNTL PFKSPSVLSI FGYDAISGLN TSADNADLWP
SSVSNTQVYA PPDGRTFGYL DFVQFSASVM GPQDYMPSIA LNGTLISGGG SGGVTPSSII
SPHEAILRYA LSHGTFPYAN FYSQNPVVLN PGGPCIVLIN TQSIESADRH ELSDDYSDTL
VTNVAKQCNN TVVVIHNAGI RLVDNWIENE NVTAVIYAHP AGQATGDALV SILWGETSPS
GRLPYTVAKK ESDYGALLHP TYPTTEHPQY AQSDFDEGVV IDYRHFLKEN IEPRFPFGFG
LTYSNFTYSN LSLTQHPEVD RSIVPCDIPT NSSSPHPEGG LDSLYDVLTT IRVTVENTGE
VEAAEVAQLY LSIPGSAAER VLRGFEKKVL QKGEKAEFTF DLRRRDLSLW DSGLQSWVLG
QGVFGVMVGR NVLDTEGLTG GFEL
//
