ID A0A3F3Q8R2_9EURO Unreviewed; 781 AA.
AC A0A3F3Q8R2;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, 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=BDQ94DRAFT_177258 {ECO:0000313|EMBL:RDH35126.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH35126.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH35126.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH35126.1,
RC ECO:0000313|Proteomes:UP000253729};
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 (JUL-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; KZ852041; RDH35126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3Q8R2; -.
DR STRING; 1341132.A0A3F3Q8R2; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000253729; 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, ECO:0000313|EMBL:RDH35126.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..781
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017549473"
FT DOMAIN 700..769
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 781 AA; 85377 MW; 130C66E38B7436E1 CRC64;
MVAGLVAKAL LLLQLGSGVV AAQNASRPLY KNPHAPVEAR VCDLLSRMTI EDKMSQLMQG
DVGNWMDSTT GAFNYTGLVE NMEMKAGAFY IGYAVPWDWL ATNIKRAQDY LLQNTTLGIP
ALVQTEGIHG FLLENATIYN SPIAYACSFN RELVEKMGRL IAQEARAIGT TQLFAPLADL
ARELRYGRVE ETFSEDSYLA GEMAYHYIVG LQSLNVSATV KHFVGYSLPE QGLNTAPVQG
GERYLRSTWL PSFKRAIVDA GAWSIMSAYH AYDGIPAVAD WFTLTKILRQ EWNYDYYVIS
DSGATDRLCT AFKLCRSSPI DMEAVTTQAL PAGNDVEMGG GSFNYQKIPE LVESGQLDIE
VVNTAVSRVL RAKFEMGLFE NPYPAAPQSE WNKLIHSPEA VELARTIDKE SIVLLENHNE
TLPLKKSGNI AVIGPMAHGF MNYGDYVIYG SQWRGVTPLD GIKAAVGDAA TVNYAQGCER
WSNDQSGFDE AIAAAKKSDV AIVVVGTWSR DQTELWENYN ATTGEHVDLD SLALVGAQGP
LIQAIRDTGV PTIVVLSSGK PITDVTWIAN STSALVQQFY PSEQGGNALA DVLFGDYNPS
GKLSVSFPHY VGDLPIYYDY LNSARNIGDA GRAYPNGTLE FGHQYVLGDP HAVYPFGYGK
SYSTFEYSDI KVSKTNVSAS DTVTVSLEVK NLDESREATE VVQVYVVDEI ASVVVPNRLL
KGFEKVVIPA GGSKSVSIDI KVEDLGLWNN KMEYVVEKGE FGVLVGSSSV DIRGRVAFWV
V
//
