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Database: UniProt
Entry: A0A0G2FXR0_9EURO
LinkDB: A0A0G2FXR0_9EURO
Original site: A0A0G2FXR0_9EURO 
ID   A0A0G2FXR0_9EURO        Unreviewed;       718 AA.
AC   A0A0G2FXR0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=UCRPC4_g05895 {ECO:0000313|EMBL:KKY16558.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY16558.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY16558.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY16558.1};
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.
RN   [2] {ECO:0000313|EMBL:KKY16558.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY16558.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC       involved in the degradation of cellulosic biomass. Catalyzes the last
CC       step releasing glucose from the inhibitory cellobiose.
CC       {ECO:0000256|ARBA:ARBA00024983}.
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:KKY16558.1}.
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DR   EMBL; LCWF01000160; KKY16558.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2FXR0; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000053317; 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:UP000053317};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..718
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002544485"
FT   DOMAIN          641..707
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   718 AA;  78920 MW;  FE128CB006651835 CRC64;
     MKSSLIQWSL LLLQSSRSSA YTSWSYTNES EVPYYGLSPP VYPSPVSNGS SSSVWAAAYA
     KANAVLSALT LEEKVNRTRG FVDTCIGNTG SVPRLGIESL CLSDAPDGIR GQEYVSAFPA
     GIHIATTWDR SLMYEYGQAL AEEYRDKGIN IALAPVAGPL GRLARGGRNW EGLSADPYLA
     GIGMGRITKG IQDIGVIATP KHFLLNEQEF RRNPADGEGE AMSSNADDRT IHELYVFPFM
     DALREGAAAV MCSYNRVNNS YACQNSKLLN GILKTELGFE GLVISDWNGQ HSGVASANAG
     LDLVMPDGGF WGGNLTEAVN NGSVSVDRLD DMVRRQLAAY FLLGQDKQYP QPSIYSNTQK
     HTPVNAQGDH GKLIRYEVNW GWNTFNGTLI TGGGSGSNSP PYVITPFQAI QERIIKDNGM
     IRWDFHSENP YPPYVNADAC LVFINAYASE SFDRTTLNDT FSDNLVNSVA ANCSNTIVII
     HSAGIRTVDA WIDNENVTAV LFAGLPGQES GHALVDVLWG DVTPSGKLPY TIAKEQIDYG
     TLLNSTISFD AFPQDNFTEG LYIDYRSFDK RNVEPRFEFG FGLSYTTFRY SKVHVVSTNY
     STSSLPDPNI SIKQGGHPDL WQILFNVTVD ITNEGDVFAH EVPQLYVTIP NAPIRQLRGF
     DRVAVNPGET NTVTFSLMRR DLSIWDIEAQ QWRLQTGDYP IYVGASSRDL RLNATLSI
//
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