ID A0A5N5JYD4_9PEZI Unreviewed; 868 AA.
AC A0A5N5JYD4;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 7.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=GE09DRAFT_1258105 {ECO:0000313|EMBL:KAB5523094.1};
OS Coniochaeta sp. 2T2.1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1571157 {ECO:0000313|EMBL:KAB5523094.1, ECO:0000313|Proteomes:UP000325492};
RN [1] {ECO:0000313|EMBL:KAB5523094.1, ECO:0000313|Proteomes:UP000325492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2T2.1 {ECO:0000313|EMBL:KAB5523094.1,
RC ECO:0000313|Proteomes:UP000325492};
RX PubMed=31572496;
RA Mondo S.J., Jimenez D.J., Hector R.E., Lipzen A., Yan M., LaButti K.,
RA Barry K., van Elsas J.D., Grigoriev I.V., Nichols N.N.;
RT "Genome expansion by allopolyploidization in the fungal strain Coniochaeta
RT 2T2.1 and its exceptional lignocellulolytic machinery.";
RL Biotechnol. Biofuels 12:229-229(2019).
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:KAB5523094.1}.
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DR EMBL; VSMA01000033; KAB5523094.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5JYD4; -.
DR Proteomes; UP000325492; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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:SF12; BETA-GLUCOSIDASE A-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:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KAB5523094.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000325492}.
FT DOMAIN 790..858
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 743..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 94130 MW; 37ADCEC86CA0F77F CRC64;
MLLSKSSRLL LGIVAIQKAN TEQLQGRAEL ATSAPYYPSP WMDPNADGWQ DAYAKAKAFV
SQMTLAEKVN LTTGVGWQGE QCVGNVGAIP RLGLRSLCMQ DSPVGVRFGD YSSVFTSGQT
AAATFDKSIL YQRGKALGQE HKGKGVNVLL GPVAGPLGRA PEGGRNWEGF SPDPVLTGIA
MAQTIKGIQD AGVIACAKHF IANEQEHFRQ TGEARGYGYN ISETLSSNID DKTMHELYLW
PFADAVRAGV GSIMCSYQQI NNSYGCQNSK SLNGLLKDEL GFQGFVMSDW QAQHTGAASA
VAGLDMSMPG DTEFNTGLSY WGTNLTIAVV NGTVPQYRID DMAMRIMAAF FKVGNTIEQP
PINFDSWTKD TYGPIHYAAN AGFQQVNWHV NVQQDHANQI RDTAAKGTVL LKNNGVLPLN
KPKFVAVIGE DAGGNPAGPN GCDNRGCDDG TLGMAWGSGT AEFPYLITPD AALQAQAIKD
GSRYESILVN NNPKAVQALV SQANATAIVF VNADSGEGFI NIDGNEGDRK NLTLWKEGDQ
LIKNVSSWCP NTIVVIHSTG PVLVTDWYNS TNITAILWAG VPGQESGNAI TDILYGKANP
SGRNPFTWGA TRESYGTDVM YEPNNGNGAP QDDFTEGVFI DYRYFDKHDT PLIYEFGYGL
SYTTFEYSNI QVKKSNAGTY KPTTGQTSPA PTFGNFSRNL GDYLFPADVT PVWQYIYPYL
NSTDGKEASK DPQYGQTAEE FLPPHATDST AQPLLPSSGK SQPGGNRQLY DTLYTVTADI
KNTGSIVGNE VPQLYVSLGG PDDPKVVLRD FDRIRINPGQ TAQFRATLTR RDLSNWDVVA
QDWVVSSYPK KAYVGRSSRK LELSADLV
//
