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Database: UniProt
Entry: A0A010QVV1_9PEZI
LinkDB: A0A010QVV1_9PEZI
Original site: A0A010QVV1_9PEZI 
ID   A0A010QVV1_9PEZI        Unreviewed;       877 AA.
AC   A0A010QVV1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   22-FEB-2023, entry version 36.
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=CFIO01_01111 {ECO:0000313|EMBL:EXF80740.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF80740.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF80740.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF80740.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
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:EXF80740.1}.
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DR   EMBL; JARH01000415; EXF80740.1; -; Genomic_DNA.
DR   RefSeq; XP_007595507.1; XM_007595445.1.
DR   AlphaFoldDB; A0A010QVV1; -.
DR   STRING; 1445577.A0A010QVV1; -.
DR   KEGG; cfj:CFIO01_01111; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000020467; 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; 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: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.
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:UP000020467};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..877
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001456259"
FT   DOMAIN          800..868
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   877 AA;  93981 MW;  5D1D5B1F1A087DC3 CRC64;
     MRTQNLVVAL LAAADQIAAA VAPEGKLHKR DLAHSPPVYP SPWMDPSADG WADAYAKAKD
     FVSQLTLLEK VNLTTGVGWQ GDVCVGNVGS VPRLGLRGLC MQDGPVGIRF TDYNSVFPSG
     QTVAATWDRS LIYRRAEAIG FEHRSKGIDV VLAPVAGPIG RAPTGGRNWE GFSVDPYLTG
     IAMAESVKGI QQHAIACAKH FVGNEQEHFR QAPEAIGYGY NITESISSNI DDKTMHELYM
     WPFADAIRAG VGSIMCSYNQ VNNSYGCQNS KLLNGLLKEE LGFQGFIMSD WQAQHAGAAT
     AVAGLDMAMP GDVLFNTGTT FWGTNLTVAV LNGTVPEYRL DDMALRIMAA FFKVGFEVES
     VPELTFSSWT KDTVGPVQYY AKENPQVINQ HVDVRKGRDH ANLIREIAAK ATVLLKNEGA
     LPLNKPKFLA VIGEDAGPNL KGPNGCDNRG CNDGTLGAAW GSGTAEYPYL VTPDQGLSAR
     AVADGTRYES ILSNYDTAAT KALVSQADAT AIVFVNANGG EGFINVGGNE GDRQNLTLWN
     AGDELVKNVS AINNNTIVVI HSIGPVLLTD MVNNPNITAI VWAGLPGQES GNSIADVLYG
     NVNPGGKSPF TWGPNRESYG ADVLYEPNNG EAAPQDDFTE GVFIDYRHFD RATAGSNSSG
     IAPIYPFGFG LSYTTFEYSN LAVTKGNAGA YAPTTGETAA APTFGNYSTD PAEYVFPSNE
     FRYIYNFIYP YLNTSDVKES ANDPTYGKTA EEFLPPNAVA STPQPKHPAS GAPGGNPQLW
     DVLYTVTATV TNTGKVAGDE VAQLYVSLGG PEDPVKVLRG FERIPIEAGA SATFKAEITR
     RDLSNWDTAS QNWVISEYPK KVWVGSSSRD LPLSASL
//
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