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Database: UniProt
Entry: A0A135S980_9PEZI
LinkDB: A0A135S980_9PEZI
Original site: A0A135S980_9PEZI 
ID   A0A135S980_9PEZI        Unreviewed;       644 AA.
AC   A0A135S980;
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|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=CNYM01_01022 {ECO:0000313|EMBL:KXH32474.1};
OS   Colletotrichum nymphaeae SA-01.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH32474.1, ECO:0000313|Proteomes:UP000070054};
RN   [1] {ECO:0000313|EMBL:KXH32474.1, ECO:0000313|Proteomes:UP000070054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-01 {ECO:0000313|EMBL:KXH32474.1,
RC   ECO:0000313|Proteomes:UP000070054};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL   Submitted (FEB-2014) 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:KXH32474.1}.
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DR   EMBL; JEMN01001582; KXH32474.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135S980; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000070054; 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 2.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 1.
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.
DR   PROSITE; PS51820; PA14; 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}.
FT   DOMAIN          210..362
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   644 AA;  70871 MW;  78E056F624E41390 CRC64;
     MIWHSYNKVD GTFCSEHGPL IEGVLRKEWG FEGIVMSDWF AVHNVVEPVK AGLDLEMPFP
     VFRGKRLAEA VRSGHITEAE IDARAIKMLE LRNRTRTSFN DEPERSEISE ETNKISRELA
     ASGIILLKND NQALPINPAD KPKVALIGEF AGSPVVTGGG SASCTPQYRH SPYKVLKEAF
     SGEESVRYHA GVRTRRVIPL VPTAQLTAQD GRHGIDVKYY NDDTPEPTLT EFQEKSNVWM
     LGEFKGGLKV PGSRIELLTK LTPQTTGEHT LAVQATGDFS LVVDGKEILS GPQKEIATEQ
     FIFNHVKLET RVQLQMNAGQ AYDIKLTNKS WDHLVKGEPT PYAASIGFEE HRSDEAAIAE
     AVELAKTSDV SIIYAGRNEQ YESEGYDLED IRMPENQTVL IKAVAAVSKK TVLVLHCGNP
     IDVSAVVDDV DAILNAHFPG QEGAQATADI LTGATNPSGR LATTWFRTLE DAPTYGDFPA
     TKQEDGTHKF RYAEGLGMGY RHAEAAKRSR FPFGYGLSYT TFTLSDLTTS VVGADKDAKL
     KVSVKVTNSG SRAGKEVVQL YVNPAKETPT SVWRPERELK AFKKVLVQPG ESAVVELEVD
     AKMACSYWDE AEKAWRLERG TYGVRVGELQ GEFSISEGTT WGGL
//
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