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Database: UniProt
Entry: L2F9W0_COLFN
LinkDB: L2F9W0_COLFN
Original site: L2F9W0_COLFN 
ID   L2F9W0_COLFN            Unreviewed;       657 AA.
AC   L2F9W0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=CGGC5_15078 {ECO:0000313|EMBL:ELA23122.1};
OS   Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS   (Colletotrichum gloeosporioides (strain Nara gc5)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA23122.1};
RN   [1] {ECO:0000313|EMBL:ELA23122.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA23122.1};
RA   Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT   fructicola.";
RL   Submitted (AUG-2012) 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; KB021441; ELA23122.1; -; Genomic_DNA.
DR   RefSeq; XP_007287847.1; XM_007287785.1.
DR   AlphaFoldDB; L2F9W0; -.
DR   STRING; 1213859.L2F9W0; -.
DR   EnsemblFungi; ELA23122; ELA23122; CGGC5_15078.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
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   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; 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          212..365
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   657 AA;  72056 MW;  425EB53E8F2CF389 CRC64;
     MTSYPKVNGA YVDDQTTFLK DILRDEWKFK GLVMTDWGAA SAAVANGIRN GLDLEMPGPP
     HRRQPAVVHK LIEDGKVDVE DIDDRVLPLL RLLRQTGKFT DRREPVPERA ISRPEHEKLI
     REAGGEGVVL LKNSDGTLPL KPSHLQNIAV LGPLAKHAAA HGGGSASLNC HYKISPFDAI
     KSRLPDSKLS YSKGAHVFRA YPDFVAGTKN RLGNSGFAAD FYENLDLIGK PFYTEEYPRG
     SFITLMNDNV VSAKSARLST DYSPDISGKH YLSFSGMGPA RLFINGEFQG EIKETAEAMS
     FLLGVQEEQH LQYDFVVGKT YSIVIESTIS PVPNAELYLA DDQIAVHLGF VSQQEMEADL
     LSEAVSFATD ADVALIFVGN TPQWETEGQD MATMTLPADG SQDKLIAEVA KVNSNTIVVI
     TTGVPVELPW LDNVAAVVQA WYGGQETGNS ILDVLLGEVN PSGRLPMSWP KKNEHTACYG
     HFGLDSWDSR EVEYVEGVNV GYRHFDSQYG TEREVLFPFG YGLSYSTFEH SACVLSGTLD
     VNDENAKITV AVTVHNTSDV AGSEVVQVYV TPPKSRTGVE RPPKSLVAFD KIHLNPGAQK
     EIQLSFKRDG AAFWSEAGRL WEVEAGEHEV HVSTSSCPKD IKSTLVLDVT EGFTFRP
//
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