ID A0A0D1Z1X4_9EURO Unreviewed; 787 AA.
AC A0A0D1Z1X4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Probable beta-glucosidase G {ECO:0000256|ARBA:ARBA00039579};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase G {ECO:0000256|ARBA:ARBA00041276};
DE AltName: Full=Cellobiase G {ECO:0000256|ARBA:ARBA00041601};
DE AltName: Full=Gentiobiase G {ECO:0000256|ARBA:ARBA00041808};
GN ORFNames=PV11_03420 {ECO:0000313|EMBL:KIV87904.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV87904.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV87904.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV87904.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN846951; KIV87904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1Z1X4; -.
DR STRING; 1016849.A0A0D1Z1X4; -.
DR HOGENOM; CLU_004542_2_3_1; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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:SF19; BETA-GLUCOSIDASE G-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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..787
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002237414"
FT DOMAIN 702..774
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 787 AA; 84611 MW; AAF86202BC7919B0 CRC64;
MLSHAVWIGL LASSTAFAQD YSTSPAVYPS PPTQGIDWET AFAQAQAFVS NLTLEEKAQL
VTGTSGPCVG NIGAIERLGF DGLCLQDGPL AIRQATYASV FPAGLTTAAS WDRNLMYQRG
FFMGTEFRNK GAHVALGPVV APLGRSAYDG RNWEGFSPDP YLTGVAAEET ITGMQDTGLQ
ACLKHFIGYE QETQRNPSLS PDNVTIESVS SNIDDRTIHE LYLWPFANGV HAGVSSIMCS
YNRINGSYAC QNSKTLNGIL KDELGFQGYV MSDWGGTHSG VASVNAGLDM NMPGPISSDQ
NSSYFGGNVT QAVNNGTVNE TRLDDMAQRI MTPYFFYNQT HYPPIDGEEP ALASSFPPYI
YQFTLGPANV DVRGEHSVLI RTLGAAGTVL LKNVNNTLPL NAPKTIGIFG NDAGDLVDGE
YFSGPAFQSQ YGYEYGNLPV AGGSGTGRLS YLVSPLEAIK ARSFQDGTLV QYILNNTLIT
TPGGLATILP VPEICFVFLK TWASEGIDRV GLEADWNSTG VVNAVASFCN NTVVVTHSGG
LNVMPWANNP NVTAILAAHL PGQESGNSLV DILYGVVNPN GKLPYTIAFN ESDYDYAPIT
NSTELLETED PSAWQSNFTE GLLIDYRHFD YYNISVAFEF GFGLSYTTFE MSSMTIQTVA
VGNISAFPDA SPIVPGGNPS LWGILYNVNV TVTNTGNVTG LTVPQVYLSL PQAAGEDPTP
LNVLRGFEKI NLEAGQSQSV ILPLARRDLS YWDTGLQQWI IPSGSIGINA GFSSRDFRQS
SQITVVT
//
