ID A0A319EHZ9_ASPSB Unreviewed; 781 AA.
AC A0A319EHZ9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BO78DRAFT_361654 {ECO:0000313|EMBL:PYI09907.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI09907.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI09907.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI09907.1,
RC ECO:0000313|Proteomes:UP000248423};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; KZ826324; PYI09907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319EHZ9; -.
DR STRING; 1448318.A0A319EHZ9; -.
DR Proteomes; UP000248423; Unassembled WGS sequence.
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; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-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:UP000248423};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..781
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016359629"
FT DOMAIN 700..769
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 781 AA; 85492 MW; 7F4184C1E0658CF1 CRC64;
MVAGLLTKGL LLLQLGSGVV TAQNASRPLY KNPNAPVEAR VSDLLGRMTL QDKMAQLIQG
DISNWMDTTT GAFNYTGLVE NMDMKAGMFY VGYAVPWDWL STNIKRAQDY LLQNTTLGIP
ALVQTEGIHG FLLENATIYN SPIGYACSFN KELVRKMGQL IAQEARAVGA TQLFAPLADL
ARELRYGRVE ETFSEDSYLA GEMAYSYIKG LQSLNVSATV KHFVGYSLPE QGLNTAPVQG
GERYLRSTWL PSFKRAIVDA GAWSVMSAYH AYDGIPAVAD WFTLTKILRE EWGYKYWVFS
DSGATDRLCT AFKLCRSSPI DMEAVTMMAL PAGNDVEMGG GSYNFQKIPE LVESGQLDID
IVNTAVSRVL RAKFEMGLFE NPYPAAPQSE WHKLIHTPEA IELARTLDKE SIVLLENHNT
TLPLKKSGNI AVIGPMAYGY MNYGDYVIYG SQWRGVTPLD GIKAAVGDSA TINYAQGCER
WSNDQSGFDE AIAAAKKSDV AVVVVGTWSR DQTELWENYN ATTGEHVDLD DLSLVGAQGP
LIRAIRDTGV PTIVVLSSGK PLTDVTWIAN STSALIQHFY PSEQGGNALA DVLFGDYNPS
GKLSVSFPHF VGDLPIYYDY LNSARNIGDA GRAYPNGTLD FGHQYVLGDP HAVYAFGYGK
SYSTFEYSNI QLSKTNVTLA DTVTVSVDVK NLDESREATE VVQVYVVDEI ASVVVANRLL
KGFEKVVIPA GESTNVQVDI KVEDLGLWNV SMKYVVEKGA FGVLVGSSSL DIRESAVFYV
E
//
