ID A0A1L7WSE0_9HELO Unreviewed; 652 AA.
AC A0A1L7WSE0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN ORFNames=PAC_05582 {ECO:0000313|EMBL:CZR55694.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR55694.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR55694.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR55694.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-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 ECO:0000256|RuleBase:RU361161};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR EMBL; FJOG01000007; CZR55694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7WSE0; -.
DR STRING; 576137.A0A1L7WSE0; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000184330; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 3.
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; IPR019800; Glyco_hydro_3_AS.
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:SF3; BETA-GLUCOSIDASE B-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 2.
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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000184330}.
FT DOMAIN 572..642
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 652 AA; 71499 MW; FE307A845BF55562 CRC64;
MSSVPHSQDN VNIDSLLTQL TIDEKISLLA GANVTDGPNG ARGSQFFDGT TVACLPAYVS
IAATFDRELT KRIGVALDQE SQTIGTYVLG PTVCSHRSSL GGRNFEAFSE DSPLSGVLAA
EHVKGLESER VGTTIKHFLG NEGIYLPPFE IVVKTADPWC LEFLQNILRQ EWKYPGLVMS
DWGATTSTAE SLNAGVDLEM PVEQIKPAIE VGTVTENAIN DRARAVLELP QKTGKSVDRK
VDIAEIVADL LEHRKLIRQA GAEGIVLLKN AENVLPLDRS KCKEIALLGP LARYAAAHGG
RKGKLGVRFT TTYTPTITSS PYLSFSTKGP SKLYINDTIL FEQPYATKDS MSFLLSVQDE
LQSQYPLEAR KSYKIRIDTI PSPEPNGELY LLDGQIAAHL DADVAIVFVG NTAQWETEGQ
DMDDMNLPAD GPQDRLIAAV AAVNPRAIAW YAVLESGNAI FDVLFEAVNP SGRLLISWLK
EYEHTAVYRN FDMDSYQSRQ VEYVEGVFVG YRHFDRMWGT EKEVRWPFGF GLSYTNFQIT
NAKVEGGLDD SGSSGLVITA DVENVGCVAG AEVVQVYLLP PSSGSEKQPV KSLAGFTKTR
LEICEKRNVF VSIILGRRLT GMLREGNGRW MRAHTGWVSM SSSPVDKKAE LK
//
