ID A0A319DXJ8_ASPSB Unreviewed; 761 AA.
AC A0A319DXJ8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BO78DRAFT_465048 {ECO:0000313|EMBL:PYI00845.1};
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:PYI00845.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI00845.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI00845.1,
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; KZ826433; PYI00845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319DXJ8; -.
DR STRING; 1448318.A0A319DXJ8; -.
DR Proteomes; UP000248423; 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:SF14; BETA-GLUCOSIDASE D-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:UP000248423};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..761
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016348148"
FT DOMAIN 677..746
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 188..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 82209 MW; F3B03CBDDC6E26CA CRC64;
MRDLTLFAAT ALLGLAAASP SSSTLGLLNY NGVALGDWES AYDKASAFVG NLTTEQKLAL
ITGSSVTSAT NESFSALVFA DGDMGLQDFN YVSAFSLASA IAMTWDQDAY YEQAKAVGIE
FYKKGIQVLN APTSQPIGRT PWGGRFGETF GPDPYLNGLA TGLAVKGYVD TGVISGAKHF
LLYEQETNRT NDPSSIGPNP ASGPLPYSSN TDDKTLHETY LWPFYDAVKN GLGAVMCAMT
KVNNTLACQN SDLLLKHLKT ELGFPGLVYP DTKAQSTETA ETVNNGEDYG DSTYWSTSVM
KALLANGTLS EARLNDMTIR NVIGYYYSNL DNGLQPAEQG DGAFVDVRGN HSKLIRKYGA
QSMALLKNKN NALPLKTVRR MSIFGAHAGA TVAGPNQDLS IDGSGPTYQG HLATGSGSGL
ASFPYLVTPL VPLTVKATED GTILNWILKD NYTSTAGSSL IPSVSGSTAV SPSYETYAGN
SDVCLVFLNA LSGEGEDRTE LYNADQDKMV NTVADNCNNT IVVINTVGPR LLDQWIEHEN
VTAVLYGSLL GQESGNSIVD VLYGDVNPSG RLIYSIPKNE SDYNVGLCYT SQCNFTEGVY
LDYRYFDAHN ITTRYPFGHG LSYTSFSYSN LTILKETPRI PASPTGNLTV GGYSDLWDTV
NSISVTINNT GSLSGAEIPQ LYLSFPSSAD QPLRQLRGFE RVDLATGEQK TVTFNLRRRD
ISYWNVVEQQ WLVAAGEYKV YVGASSRDFK LHGSFMVRTH V
//
