ID L2FFC1_COLFN Unreviewed; 815 AA.
AC L2FFC1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Probable beta-glucosidase G {ECO:0000256|ARBA:ARBA00039579};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase G {ECO:0000256|ARBA:ARBA00041276};
DE AltName: Full=Cellobiase G {ECO:0000256|ARBA:ARBA00041601};
DE AltName: Full=Gentiobiase G {ECO:0000256|ARBA:ARBA00041808};
GN ORFNames=CGGC5_13947 {ECO:0000313|EMBL:ELA24756.1};
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:ELA24756.1};
RN [1] {ECO:0000313|EMBL:ELA24756.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA24756.1};
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 -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose.
CC {ECO:0000256|ARBA:ARBA00024983}.
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; KB021241; ELA24756.1; -; Genomic_DNA.
DR RefSeq; XP_007286193.1; XM_007286131.1.
DR AlphaFoldDB; L2FFC1; -.
DR STRING; 1213859.L2FFC1; -.
DR EnsemblFungi; ELA24756; ELA24756; CGGC5_13947.
DR HOGENOM; CLU_004542_2_3_1; -.
DR OrthoDB; 5486783at2759; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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:SF19; BETA-GLUCOSIDASE G-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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..815
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003958075"
FT DOMAIN 729..801
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 815 AA; 88001 MW; 23079661B4FE7471 CRC64;
MTAALSLILS GLLLAPAVNG QAYDAGERGE DAFEYVQPLN TTILGPYGHS PAVYPSPNTT
GNGWEDALAK AKAFVNELTI EEKADMVTGQ PGPCVGNIVA VPRLGFNGLC LQDGPLSIRV
ADYASVFSAG VSAAATWDKD ILYERGYAMG KEFKAKGAHV ALSPVAGPLG RSAYSGRNWE
GFSPDPYLTG IAMYQTITGH QDAGVQATAK HWIGNEQETM RNPTFDPNGT DTDITVQALS
SNIDDRTIHE LYMWPFANAV KAKAASFMCS YQRINGSYGC QNSKSLNGLL KTELGFEGYV
MSDWGATHTG VAAIEAGLDM DMPGGLGSYG QAWASGSFFG GNVTLAVNNG TLDVARVDDM
ILRIMTPYFW LGQDKDFPSI DPSSGDLNTF SPKSTWVREF NLTGERSRDV RDNHGEIIRK
HGAAASILLK NENKALPLKA PKSIAVFGND AGEDTQGFYN QKDFEYGTLV AGGGSGTGRL
TYLVSPLEAI KARAAQDGAL VQQWLNNTLI INSNMSDLWI PKTPEVCLVF LKTWAEEAAD
RQHLDVDWNG NDVVEAVAKD CNNTIVITHS SGINTLPWAD HPNVTAILAN HYPGQESGNS
LIDVLYGDVN PSGRLPYTIA LNGTDYNAPP TTAINTTGEY DWQSWYDEKL EIDYRYFDAK
NITVRYEFGF GLSYTTFELA DFAAEAVADN ITSAPEERPV EPGGNPALWE TIFNATVTVS
NSGDVEGAAV PQLYVSFPAD TTPAGTPPKQ LRGFEKVPLA VGASKTIGFE LMRRDLSYWD
VVSQQWVIPA GEFTLSVGWS SRDLKASTTI TPVQA
//
