ID A0A166STH9_9AGAM Unreviewed; 920 AA.
AC A0A166STH9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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};
DE Flags: Fragment;
GN ORFNames=FIBSPDRAFT_778405 {ECO:0000313|EMBL:KZP29809.1},
GN FIBSPDRAFT_791242 {ECO:0000313|EMBL:KZP19075.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP29809.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP29809.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP29809.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR EMBL; KV417567; KZP19075.1; -; Genomic_DNA.
DR EMBL; KV417497; KZP29809.1; -; Genomic_DNA.
DR STRING; 436010.A0A166STH9; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000076532; 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 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:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KZP29809.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000076532};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..920
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007997432"
FT DOMAIN 840..909
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 37..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 920
FT /evidence="ECO:0000313|EMBL:KZP29809.1"
SQ SEQUENCE 920 AA; 96349 MW; 554A7AAF8F5F4470 CRC64;
MKSPLSVSLL PWLLLATSVA ADLNTHAARD NIAHGHNLKR HWGGRGVDSQ KTSSTGAITS
SQLASSALSS SQKASSSSKA ASTASASGST SSKAASSSAS KSGSASSSGA SSVPAPSSSP
ASASPPLSTA SSVAVSSSAT SKSGSASGTA SASSSAASPT GTLTPSKPVN GDGGWNEAVT
RARAFVSQLT INEKVNLTTG VDTDGRCVGN SGSVPRLNFA GLCLEDSPVG VRDADYTSLF
PSGMNVAMTW DAGLMYQRGA AMGAEFRGKG VNVALGPMMN LARNAAAGRN WEGAGADPFL
AGVHAVNNIL GIQSEGVIAC AKHFALNEQE HYRGGGGGEA YSSNQDDRSF HEMQLWPFAE
SVKAGVGSVM CAYNRVNGTE SCENRHLLNT VLKEELDFQG FMLSDWAAVT SLYASVMNGA
DMNQPGFVAY GNPNDPNPAS ANNSYWGAQL GDAVRNGTIP EARFDDMVTR IMAAYYKMGQ
DTGFPAVNFD YNTENTYYEG EKVNEHVNVM GNHSILIREV GAASTVLLKN VNNALPIDFS
KVKNLAIVGS DAGPNPDGPN SCNDRGCDEG TLAIGWGSGT ANFPYLIDPL AAITAYIRSL
NPTSVVQGVL SDFNYAQVNA TAAQADTCLV FANADSGEGY ITVDGNAGDR TNLTLWHGGD
ALVLATAAHC ANTIVVMHIV GPVLVEAWFD HPNVTAILNA GIPGQETGNS ILDVLSGKVN
PSARLPFTMA KQRSDYASDI LYSVSNTSNA YIPEINYTEK LELDYKYFDA KNITPRYEFG
YGLSYTTFAY SGLSLKPAFT SAAAVPKGSA TQPGGETGLY SNALTATFTV KNTGKYDGNE
VAQLYIGFPK SAAEPPRVLR GFERSFIKQG KTAQFSIGLR VKDISIWDVI TQSWVIPTGE
FTVYVGSSSR ALHLTKTFTL
//
