ID L2FKV4_COLFN Unreviewed; 713 AA.
AC L2FKV4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=CGGC5_12122 {ECO:0000313|EMBL:ELA26972.1};
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:ELA26972.1};
RN [1] {ECO:0000313|EMBL:ELA26972.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA26972.1};
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB021007; ELA26972.1; -; Genomic_DNA.
DR RefSeq; XP_007283994.1; XM_007283932.1.
DR AlphaFoldDB; L2FKV4; -.
DR STRING; 1213859.L2FKV4; -.
DR EnsemblFungi; ELA26972; ELA26972; CGGC5_12122.
DR HOGENOM; CLU_004542_2_1_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:SF14; BETA-GLUCOSIDASE D-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; 2.
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..713
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003958464"
FT DOMAIN 632..701
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 157..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 713 AA; 75992 MW; 83933B4D3C86F5FC CRC64;
MYRPSTAWAL AILTYVTGTL AADASANYTE QLSPLLGGDG GNFTGLHNLD SATNPLTYFY
VTTWPAGLAM AMTWDTAAAE GQGQGVGVEF KGKGINMAYG PTLEPLGRSA WGGRTGETYG
VDSYQAGIMA GAVVKGMSSA GVVASAKHFI LNEQETNRMS TGSGGGMGGG SPPDGAGPGG
NSTLTRRQTS TNGTTTGNST SSDDTGAYTV TISDKAFHET YLWPFYDTVY NGMGGAMCAM
NKVNGTYSCE SQDLLAKYLK VELGFPGIVH VSAQKTGINA ANAGMDLSSS SYFSNTTLGA
GLNNGSFTMD RLDDMAIRNM MGYFHLGQDQ GYPAHAGVTD RVDNRGNHSA MAREYAANSI
ALLKNTNNAL PLVNKSSISI FGFHAGPRYG HMAVVGGSAM GSLSYLTTPL QLFNQRAATD
GFMLRWWLND TSETSFSGMS GSGTELTEST TGVADLSDAC VVFLNAWGGE GADRTELTNA
DQDTLVTTVA DVCNNTIVVI NTVGPRLVDA WIEHENVTGV LYGGALGQES GNAIDDVLFG
AVNPSGRLVH TIAKNESDYN PDTIISETEL NLDFSDGNYI DYKYFDYYNV TPRYEYGYGL
SYTTFEYSST ATVESSNLTS GFATGDKLRC REVAQLYISF PDAAGEPVRQ LRGFQKVTIQ
PGESADVTFS LRRRDLSVWD VFGQEWKVES GEYRLYVGAS SRDFKAQTAL TVA
//
