ID A0A010QJ45_9PEZI Unreviewed; 835 AA.
AC A0A010QJ45;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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_00873 {ECO:0000313|EMBL:EXF79977.1};
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:EXF79977.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF79977.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF79977.1,
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:EXF79977.1}.
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DR EMBL; JARH01000489; EXF79977.1; -; Genomic_DNA.
DR RefSeq; XP_007596339.1; XM_007596277.1.
DR AlphaFoldDB; A0A010QJ45; -.
DR STRING; 1445577.A0A010QJ45; -.
DR KEGG; cfj:CFIO01_00873; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_4_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; 2.60.120.260; Galactose-binding domain-like; 1.
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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF13; BETA-GLUCOSIDASE K-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 PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467}.
FT DOMAIN 403..562
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 835 AA; 91863 MW; 6266699FCC4CD16E CRC64;
MQPPPRKVVN VDQIIENATL AEKISLLAGS DFWHSTPLPQ HNVPAIKCTD GPNGVRGSRF
FNPMPALCIP CGSGLGATWN AELIEQAGQL LSKECDAKGA HVWLGPTVNI IRSPLNGRGF
ESFSEDPHLG GMLAAAIIRG VQSRGTLAAL KHFVANDQET EKMSLDVRMS DRALREIYLL
PFQIALRDSN PRVVMSSYNK IGGLHVSENP MILQDILRKE WGFDGLIMSD WYGTYSCEAA
LNAGVDIEMP GPSRYREKEA LAAVFSGKVH QHTIDERARK VLHFVNDAAS ARVEKEENMR
DIPEDRTLNR RLAGESVVLL KNSANLLPVS PEDCSEVAII GPNAELAAAC GGGSASLRPY
YTSSVLKGIR DSLPPTAKVH HEPGVYGHIL LPPFTEDSVC NDEGRQGVTI ELFNEPHTNK
QRRAFDRVTI PDTTYQLMDY EHPQKGETFF MSMRANFVPE HTGTYEFGLA TYGIGDLFIN
DEIVINNSTE QTPGGMFFGK GSAEKRATYD MTAGKRYHLR VEAGSATTSK VKGGSLLAIP
GGACRLGGCR KINPEEGIQR AVELAKRCKY TFVVAGLNAD LEKEGKDRDT MNMPPQVDNL
IAAVLEAQPN TIVITQAGNP ISLPWRHSAS TMLHSWYGGN EAGNAVADVI FGRINPSGKL
PMTFPARLED NPAYLGFGSD NGKVYYSEDI FVGYRWYEAR KMEVAFPFGH GLSYTTFQIS
EIQVSSSRVY FSIENTGRMA GAEVARLYIS YSTTSPKSRF SRPVRSLTGF EKVFLQPGEK
KSVSIPIDRY STAVWDEKKN SWCCERGRYT ASIVAGGAIL DGSFEIEKET FWNGL
//