ID A0A1F8A895_9EURO Unreviewed; 802 AA.
AC A0A1F8A895;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=ABOM_002794 {ECO:0000313|EMBL:OGM47944.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM47944.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM47944.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGM47944.1}.
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DR EMBL; LYCR01000019; OGM47944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8A895; -.
DR STRING; 109264.A0A1F8A895; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000179179; 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:UP000179179}.
FT DOMAIN 717..789
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 802 AA; 87269 MW; F2E6D87B08DB65EB CRC64;
MRSELVYTAA FASCIGASGA VRNHNDYLYS PTPDEIPNPD ATGLEWEDAF ARASDFVSQL
TTEEKVSLVS GTEGPCVGNI APIYCLNFTG LCIQNGPLAL EQGTYSSVFP AGITIAATWD
KNIAYERGSQ MAAEFRGKGS QVLLGPVAGP LGRSGLGGRN WEGFSPDPYL TGELFTETIL
GIQDTGVQAC AKHFIGNEQE TQRQPSQNED GTTIESVSSN IDDRTMHELY LWPFQQAVRA
GVATVMCSYN RLNQTYGCQN SKVLNGILKE ELGFQGYVMS DWGATHSGAF AINAGEDMDM
PGTASFGTVF FHENLIESVK NGSVSMDRLD DMCRRVMTPY FHLNQDKDFP GLDPANKELN
AVLFSSPQEY KYNYTYGPVA NVDVRGNHGE EIRKQAADGT VLLKNTNNTL PLKSPKQIAV
FGNDAGDFTN GMSVFYFNGV GDYEYGVLAA GGGSGSGLFS YLVSPLEAIK QRAGFRDQTL
VQYVLNNSAI IEEDSPYLKA LLPSSPDVCL VFLKSWATEG EDRASLRVDW NGDEVVEKIA
STCSNTVVVT HSNGINVLPW ADHPNVTAIL AAHLPGQEAG NSIVDVLWGD VNPSGHLPYT
IAKTQSDYSF APIQNATALQ DTNDPAAWQS DFKEGVLIDY RHFDYYNKTV QYEFGYGLSY
TTFSIGKNIS ITPLFNGDLS ALPADAKVVP GGNPNLWEAL YRISITVKNT GEVAGAAVPQ
LYLGLPKETT RAASPVNVLR GFEKVYLQPG ESRKVTFELT RRDISHWDVT GQQWAIASGV
MQAHVGFSSR DFQVASSFTP IR
//
