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Entry: A0A1Y1VBN0_9FUNG
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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}.
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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
//
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