ID A0A0M8MYP6_9HYPO Unreviewed; 790 AA.
AC A0A0M8MYP6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=ESCO_005887 {ECO:0000313|EMBL:KOS17064.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS17064.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS17064.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) 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}.
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:KOS17064.1}.
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DR EMBL; LGSR01000028; KOS17064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8MYP6; -.
DR STRING; 150374.A0A0M8MYP6; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000053831; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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; 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: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.
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 Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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:UP000053831}.
FT DOMAIN 693..768
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 640..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 85765 MW; 47D6D3C6E83A76B2 CRC64;
MLYEKELCLN DSPSGVRQAD NVTVFPAGIT TGATFDKSLM YKRGVAIGRE NRLKGVNVWL
GPTVGPVGRK PKGGRNWEGF GVDPVLQAVG GRETIRGVQE QGVIATIKHF VGNEQEMYRM
YNPVQKAYSS NIDDRTLHEL YAWPFAEGIH VGVGAAMMAY NAVNGTACSQ HPYLINGLLK
DEMGFQGFVM TDWLAHMSGV ASALAGLDMD MPGDTQIPFF GNSYWMYELT RSALNGSVPM
DRLNEAATRI IAAWYQMGQD QGFPHTNFDT NSKEAFNPLY PAAWPASPSG ITNEFVRAQA
DHDVIARQIA QEGITLLKNQ GNVLPLSKGQ PLKVFGTDAQ QNPDGLNSCR DRNCNKGTLG
EGWGSGTVDY MYMDDPISAI KADSQNVVYY NTDTFPSNSI PKPTDQDIAV VFVNSDSGEN
TYTVEGNHGD RDASGLYLWH GGDELIQKAA ANYKTVIVVI HTVGPIILEK WHDLPSVKAI
LVAHLPGQEA GRSLTNVLFG RTSPCGHLPY SITKKETDLP SSVTTLIDSE AFLAQAQDSF
TEGLYIDYRY LNKQGIKPRY AFGHGLSYTT FAFSNVSIAK GVQMSPFPPS AVPRGSSSLN
YSQAIPDAQQ AVLPAGLRPI LRYIYSHLSR SDADAAIRDG QTKTYPYPPG YSTQQKPGAR
AGGGEGGNPV LWDVAYTVTL TVTNTGATYP GKVAVQAYLQ FPTAPGSPET PVIQLRDFEK
TRELAPGEST TVTLTLTRKD LSVWDVGAQD WRIPAVDGAY KVWLGRASDA LFTVCDADTL
SCRSGAAPPV
//
