ID L8X4C6_THACA Unreviewed; 809 AA.
AC L8X4C6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=AG1IA_02003 {ECO:0000313|EMBL:ELU43962.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU43962.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU43962.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
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 -!- 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:ELU43962.1}.
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DR EMBL; AFRT01000456; ELU43962.1; -; Genomic_DNA.
DR AlphaFoldDB; L8X4C6; -.
DR STRING; 983506.L8X4C6; -.
DR HOGENOM; CLU_004542_5_1_1; -.
DR OMA; MSAYHSY; -.
DR Proteomes; UP000011668; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-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 Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000011668};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..809
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003997149"
FT DOMAIN 729..798
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 20..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 87181 MW; 919D78526E4EC8ED CRC64;
MKTVAWTGFL VAASAPVALA QGSSSTSTSH SFSTTRTTTS TTTQTSTSTS TSSPSGRPLY
KNPNAPIEDR IKDLLPRMTV EDKVAQLIQG DINGWMDMND PKDNTLTLKL VYAVTVGQKY
LMENTTLGIP AIFQSEGLHG FTNNGTIFPS PLSMACSFNN DLIRKVAEVV SNEAEPLGIT
QIFAPVLDLG RELRWGRVEE SFGEDHFING EMGLAFVEGI QSGRRLNAST TAIARMAATC
KHFAAFGTPH GGLNIAPVAG GERDLRSVYL RPFNRACLNA LSIMTAYSSY DGIPAVTNKQ
WGYKYWAVSA AANQAILKVD LPMTLHGTCD SRECCAKKAL ENGLQGEMGG GTYTYLTLPE
QIRAGKVSQT ALDETVTYML RTKFALGLFE NPYPYANYTG HVRTKETLDL LLQVERESIV
LLENHNNILP LSKTSIKSVA LIGPSLGTQL GDYVFAGAKD NAVSRAFILP HLLVISLTTP
TIALDGFKKV LAGSNVQINY AEGCKLWSAS EEGFPEAVAA AQKSDVAVVA VGTWSLDQTL
LWQGVNATTG EHVDVSDLGL VGAQLNLIKA IKATGKKVIV VYVSGKPIAE TWVYRNADAI
ISQFYGGELQ GVALAEVIFG DYNPSGRTSA SWPRSVGTAP AFYDYLKGAR PVDWTGPGRI
EDDGTLVFGH EYSLDTPVPF WSFGHGLSYT TFQYSGLKLN KSVLSATDTL VVTVNVKNTG
SRAVSHLTRS PQVYMTDVVS SVVTPVQSLQ GYTKIDLQPG QSKSVSISIP VQNLAVWTLE
NKFVVEPGKF TVQIGTSQTV HINGTVTVQ
//
