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Database: UniProt
Entry: A0A1Y2DWN1_9FUNG
LinkDB: A0A1Y2DWN1_9FUNG
Original site: A0A1Y2DWN1_9FUNG 
ID   A0A1Y2DWN1_9FUNG        Unreviewed;       839 AA.
AC   A0A1Y2DWN1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=LY90DRAFT_668266 {ECO:0000313|EMBL:ORY63609.1};
OS   Neocallimastix californiae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY63609.1, ECO:0000313|Proteomes:UP000193920};
RN   [1] {ECO:0000313|EMBL:ORY63609.1, ECO:0000313|Proteomes:UP000193920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:ORY63609.1,
RC   ECO:0000313|Proteomes:UP000193920};
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   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
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   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|ARBA:ARBA00004987}.
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:ORY63609.1}.
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DR   EMBL; MCOG01000056; ORY63609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2DWN1; -.
DR   STRING; 1754190.A0A1Y2DWN1; -.
DR   OrthoDB; 5486783at2759; -.
DR   Proteomes; UP000193920; 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 F-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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ORY63609.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193920};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..839
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010999211"
FT   DOMAIN          353..424
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   839 AA;  93395 MW;  51D215C2BA7B8F70 CRC64;
     MKFFNLIVFS LLFYNLILAS PIKKKCYAKN KKNAAENSEN SEVSEKMNQY EIDHINTLDS
     YLSECTILLR KNGDFPIGKS TKQVYLYGNG VRKTIKGGTG SGDVYSRSFD TIEQAFTKAG
     FEILSKDYLD EYDKIYTKAK DEFRKKVQSE VTDPMSLMGV IMPEPDYDIP YAKEGDLAIY
     VLARISGEGS DRQAVKGDVY LTETERKMIL DLAKGFKKFM LVLNTGGAVD LSGIDEVENI
     LLLSQLGVNT SKTLVDIITG DKYPSGKLTT TWTKYEDYPS NDNFGDNDDT DYKEGIYVGY
     RYFDTENIDV MYPFGFGLGY TDFEFDVKSA KLSGEKFEVK ASVTNVGKYK GKEVLEVYLS
     KPGTTIDEPY QILVGFAKSK ELSPKKKDDL KINFKLSDFA SYDAKTATYF LDEGEYVVRI
     GNSSRNTVPC GVIKVDKRIN VKKVENKMGK PEFEDYVPEG KRKQEDLSGV KVFKLKASSI
     KEKVVKYNDK YEISEGVKAL SNEEKAKLVI GAFQDGPASV IGSASITAAG AAGETAKVAD
     LKPVIMADGP AGLRLAKDYF IDEYGAHSTS GSMAESMVEF VPDEIKAMLI SKPEIPEGTE
     ILHQYTTAIP IGTAIAQSWN RKFAELCGDI VGSEMELFKV QLWLAPALNI HRSILCGRNF
     EYYSEDPLIS GAFAASITKG VQKHNNTFVT IKHYAANNQE TNRYLNSSNV SERALREIYL
     KGFEIAVRES QPKAVMTSYN LINGVHTSES KELTNDILRN EFGFEGIVMT DWVVGLGGNH
     KYSGPTPYNV IKATGDIYMP GSKADYEAVL KALKEGTLSI EELEMSASRI YNLSKEIFN
//
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