ID A0A1Y1VBN0_9FUNG Unreviewed; 858 AA.
AC A0A1Y1VBN0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BCR36DRAFT_350225 {ECO:0000313|EMBL:ORX52070.1};
OS Piromyces finnis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX52070.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX52070.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT biomass hydrolysis.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX52070.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) 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}.
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:ORX52070.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCFH01000016; ORX52070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1VBN0; -.
DR STRING; 1754191.A0A1Y1VBN0; -.
DR EnsemblFungi; ORX52070; ORX52070; BCR36DRAFT_350225.
DR OrthoDB; 1328897at2759; -.
DR Proteomes; UP000193719; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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:SF10; 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 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000193719};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..858
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010984272"
FT DOMAIN 373..445
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 858 AA; 96190 MW; A927AFD8A1903124 CRC64;
MKFFNLFLLG ILNTHLVLSV PVKEETTDIE ESFSEVENVT GIIDVDDIDV GVENSSDEEK
DEINEYEIEH QKIVDEHLGE CTVLLKRNGD FPLSSKERKI HLYGGGIRHT VKGGLGSGDI
ETRTFDNIET AFKKGGFEVL TKDYLDAYDE CYQNAYDAYI GQLKAEFDYE NPFGYIFSHF
SVVLNEPECD IPIQKRGDVA LFVVSRISGE GLDRVNEKGD VLLTDSEKKA IKTLAKGYKK
FMLVLNTGGP VDLSGLEEVK NILVLSQLGA NTSKALVDLV TGEKYPSGKL ATTWTKYDEY
FADIGNLTDT DYVEGVYVGY RYFDSADVDV LYPFGYGLGY TDFKNSVKNV RISGDKVTVD
ASVTNVGKFK GKEVLELYLS KPSTSELDEP YQILVNFAKS KELSPRKKDN LKLEFKLSDF
ASYDSKIQAY VLSAGNYVVR IGNSSRNTVP CAVIEVPSKV IIKKVQNQLT EPEFKDLVFQ
SKKRDDLRGV KRLRLNVKSI KTETVDYSKK FRINEEVKAL STEEKVKFVI GAHSEDPFGS
YATTVAGIAG ELYKFKDLKP VVLSDGPAGV NIARDYYIGE DGLPHATKGG IPFTALEVVP
DDIKGQFGFL FPKAPEGVKL YHQYTTAIPI GTALAQSWNV NFAQQCGDIV GTEMSMFHIN
LWLAPALNIH RSILNGRNFE YYSEDPYVSG IMATYVTKGV QKHKNAFVTL KHYAANNKET
NRYGSSSNMS ERAFREIYLR GYEIAIKNAN PKGIMSSFNL INGIHANQHI GVIANILRRE
NNYNNVIMTD WTSPSMASTD KYPDYSPYEI IKSSHDVIMP GSKDYYDLVL EAVKENKLTM
EELESSVTRI YELIKEIQ
//