ID T0LYN6_COLGC Unreviewed; 775 AA.
AC T0LYN6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=CGLO_03280 {ECO:0000313|EMBL:EQB56691.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB56691.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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}.
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:EQB56691.1}.
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DR EMBL; AMYD01000679; EQB56691.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LYN6; -.
DR STRING; 1237896.T0LYN6; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_3_1; -.
DR OMA; CSKHYIA; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
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, ECO:0000313|EMBL:EQB56691.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..775
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004580436"
FT DOMAIN 691..762
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 775 AA; 83575 MW; 9AB313D0F791512E CRC64;
MFGILKGSLF LLGVHGAYAV RHASRSENNG TRDWDAAAAM ASDFVSRLTL DEKVSMITGN
SSAGNCIGVI APIPRLGFQG LCLLDGPAAI NRVDLVSVFP SGITAAATFD RDLIYRRGPS
TGPMGRHALG GRNWEGFGPD PYLAGISIAQ TVHGVQDAGV QTCSKHYIAN EQETQRSNTN
QTDGTRAEAI SANVDDRTIH ELYLWPFADA IKAGTTSVMC SYNRLNQTYS CENSHTLTKL
LREELGFQGY TVSDWFATHS TSESINAGLD MEMPGIIPSY QGSVLYFGER VLEAVSNGTV
SEARIDQMVR NIMAPYYFLG QDAEDYPTAD PALRWVTLIQ EVGLGAAKAG GFLPDDFVFE
HGRDVRGDHA KVIREMGAAG TVLVKNNNTL PLSSPKIIGV FGNDAGDMTD GFYRPSEVPD
NVNTGTMIIG GGSGTGRASY IVSPLRAIQA KAAETGAEVL YATNNELLAK NDFRGIYPPP
EICVVFQQTF ASESFDRTSF ELDGNSTAVI NNVADFCGNT IVVTHSGGVN TMPWANHTKI
GAILLAHYPG QESGNAIVDL LWGDVAPSGR LPYTVPRNEA DAGPPVVNIT GPVSDPLAWQ
ADFTEGQLID YRHHDAQDIE PLYEFGFGLT YTTFSIEDNK IAVSLVKGNS SVTVRPDASL
KTQPGGNPQL WDELVTVKAK ITNTGDRSAH AVPQLYLSYP EGAPEGTPRK VLRGFEKIMI
EPGASADVEF GVLRRDLSLW DVVEQDWVIP GGQFTFRVGF SSRDLPAETM FSVLG
//