ID A0A5N5WRR0_9EURO Unreviewed; 803 AA.
AC A0A5N5WRR0;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 8.
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=BDV29DRAFT_198019 {ECO:0000313|EMBL:KAB8070415.1};
OS Aspergillus leporis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=41062 {ECO:0000313|EMBL:KAB8070415.1, ECO:0000313|Proteomes:UP000326565};
RN [1] {ECO:0000313|EMBL:KAB8070415.1, ECO:0000313|Proteomes:UP000326565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 151.66 {ECO:0000313|EMBL:KAB8070415.1,
RC ECO:0000313|Proteomes:UP000326565};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) 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}.
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DR EMBL; ML732303; KAB8070415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5WRR0; -.
DR Proteomes; UP000326565; 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:0030245; P:cellulose 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 Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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:UP000326565};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..803
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5024854974"
FT DOMAIN 718..789
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 803 AA; 86990 MW; 19CCB1C8B3218169 CRC64;
MAPVLSTLLS SFLLATAVKA QAFDAERSED AFSHVQPADT VILGPYGHVP PTYPSPNTTG
AGGWEQALIK AKEFVSQLTI EEKADMVTGT PGPCVGNIVA IPRLGFNGLC LQDGPLAIRV
ADYASVFAAV LYQRGRAMGE EFKAKGAQIA LSPVAGPLGR SAYSGRNWEG FAADPYLTGV
AMEETISGHQ DAGVQATAKH YIGNEQETQR NPTPDPNGTI TDVLQESLSS NIDDRTIHEL
YLWPFANAVR AKAASFMCSY NRLNGTYACE NSKALNGLLK TELGFQGYVM SDWGGTHSGL
ASIEAGLDMN MPGGLGMYGQ TYHVGSYFGG NVTNAVQNAS LPVSRLDDMI IRIMTPYYWL
GQDRDFPSVD PSSADLNTFS PRATWDREFN LTGSRSRDVR GNHGELIRQH GAAATILLKN
ENNALPLKAP KSIAVFGNDA GDDTEGFYNQ ADFEYGTLSV GGGSGTGRLT YLVSPLSAIN
ARAAKDKTLV QQWLNNTLIA TSNVTDLWTP TPPEVCLVFL KTWAEEGLDR GSLDFDWNGN
GVVESVANDC NNTIIITHSS GINTLPWADH PNITAILAAH YPGQETGNSI VDVLYGDVNP
SGHLPYTIAY NASDYNAPPT TAVSTSGKYD WQSWFDEKLE IDYRYFDAHN LSVRYEFGYG
LSYTTFNLKE IQTEALVQEI TPKPEALPIQ PGGNPSLWDA LYNVTIGVSN TGDVAGAAVP
QLYVSFPSST PSGTPPKQLR GFDKVFLEAG ETKTVGFELM RRDMSYWDSI SQDWLIPEGE
FTIHVGFSSR DLKASTKLTV IRP
//
