ID A0A1Y2AT95_9FUNG Unreviewed; 876 AA.
AC A0A1Y2AT95;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=LY90DRAFT_388909 {ECO:0000313|EMBL:ORY25694.1};
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:ORY25694.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY25694.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY25694.1,
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:ORY25694.1}.
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DR EMBL; MCOG01000209; ORY25694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2AT95; -.
DR STRING; 1754190.A0A1Y2AT95; -.
DR OrthoDB; 1328897at2759; -.
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};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..876
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013005559"
FT DOMAIN 392..463
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 29..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..80
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 98420 MW; FC086826F10563E2 CRC64;
MRIFNIFLIG IILNIYLVLS NPAEKAETSD ISEAENLSDG ENEEVNVNVD DNDIENVEED
SGVDDDEAEE EVENETNENE MSEYEIEHIN MLDEYLGEST VLLRRNGDFP LAENERKIYL
YGNGIRKTIK GGTGSGDINI RKFDNIETAF KNEGFEILTN DYLDAYDVCY QKAYDAYINK
LKSEFDYDNP FAYLFAHFSV ILNEPECDNL PVEKEGDVAI FVVSRISGEG VDRVNDKGDA
LLTDTERNTI LTLAKGFKKF MLVLNTGGPV DLSGLDDVKN ILVLSQLGTN TSKTLVDLVI
GEKYPSGKLA TSWTRNEDYF ASMGNLTDIN YVEGVYVGYR YFDSADVDVM FPFGFGLGYT
DFKFNFKKVK IIGDRVSVDA SVKNIGKFNG KEVLELYLSK PQTELDEPYQ QLVSFAKTDE
LAPNGEETLR LEFNMSDFPS YDSKTQSYII DKGSYIVRLG NSSRNTVPVA VIEVPSRVIV
KKVENQIGNP GFEDKVFHSK KKDSLKGVKK LKLNVKSIKT ETVDYNKKFE VSDVIKGLTT
EEKIKFVVGA HSDDPNGSYV TTVAGVAGEL YKFGDLKPVV LSDGPAGVNI ARDYFIDEAG
VHSTKGSLPE SALEIVPEDL KAMFSFLFPK IPEGTKLHHQ FTTAIPIGTA LAQSWNIEFA
ELCGDIVGTE MNMFHINLWL APALNIHRSI LNGRNFEYYS EDPLISGMMA AHITKGVQQH
KNTYVTLKHY TANNKENNRF GVSSNMSERA FREIYLRGFE IAIKKSNPGA IMSSFNLING
VHVSHHYGVI ANVLRKENNF DNVIMTDWTV QNMALSDKYP DYDLCEIIKS SHDVVMPGSK
NFYDQVTEAY KNNKLTIEEI EQSATRIYKL IKKIQE
//
