ID A0A0D9V6A0_9ORYZ Unreviewed; 1036 AA.
AC A0A0D9V6A0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR01G28050.2, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR01G28050.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR01G28050.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR01G28050.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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};
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DR AlphaFoldDB; A0A0D9V6A0; -.
DR EnsemblPlants; LPERR01G28050.2; LPERR01G28050.2; LPERR01G28050.
DR Gramene; LPERR01G28050.2; LPERR01G28050.2; LPERR01G28050.
DR Proteomes; UP000032180; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd19907; DSRM_AtDRB-like_rpt1; 1.
DR Gene3D; 3.30.160.20; -; 3.
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 InterPro; IPR044450; AtDRB-like_DSRM_1.
DR InterPro; IPR014720; dsRBD_dom.
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 PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00035; dsrm; 3.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM00358; DSRM; 3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 3.
DR PROSITE; PS50137; DS_RBD; 2.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 50..119
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 133..201
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 289..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1036 AA; 113130 MW; B1AB7FFED0711CC9 CRC64;
MYKSRLQELC QQRLWAPPEY THRRGGPDHA PLFGATVSVN GAEFENQPSS YKSQLQIYTQ
KRGKGLPLYQ TIRQGPVHSS QFKSVVTVDG EAFESPEYYH TVKEAESAAA KLALMSLPQE
ASSTEQVPVQ PLSYKNLLQE LAQKQGFTLP AYNTTSDGSV HVHIFKSTVT FQGESYQGEP
GNTKKQAEMN AAKVAFQHFE DGRNNVLSST VLTRPHLEQG TAGLSAGQQQ VKIAEPVNSV
FQASTATNHS ASGATDHDYH RLVATNPLPL ADSAKSSDED IESCELKDNK LASPEPSTVA
EEVNSAPGPE LKASDGHRPE IKPSDGHPVP LASTNAVHST GCGCSLITNR VQVYPRRPDL
VLPEGATLLP FSDDAWVAVS LPTLNHRDAE LATGADAGRI APRVWLLRGM ICRKIYLVCL
LLLLHFASMG DAAYMKYKDP KQPTNTRVKD LISRMTLAEK IGQMTQIERE VASADVMKNY
FIGSVLSGGG SVPAPQATPA IWVNIVNEFQ KGALSTRLGI PMIYGIDAVH GILTSLGGLV
KQLLLKYGQQ AFHIPLLHVC RDPRWGRCYE SYSEDHRIVQ QMTDIILGLQ GEIPINHTKG
VPYIAGKDKV AACAKHFVGD GGTHNGINEN NTIIDEHGLL GIHMAPYYDA IIKGVATVMV
SYSSLNGVKM HANNDLVTGY LKSKLHFRGF VISDWLGIDR ITSPPDANYT YSVMVPYHYT
DYINNVTSLV KKGVISMSRI DDAVRRILRV KFTMGLFESP LADLSFSDQL GKKEHRELAR
EAVRKSLVLL KNGNSPNQQF LPLPKKARSI LVAGSHADNL GYQCGGWSIK WFAASGDITV
GTTILDAIKS TVADSTHVVY SENPDESFMK ENDFSFAIVV VGEPPYAETV GDSTELTILD
PGTDTIRTVC STVKCAVVII SGRPVVIEPY LPMMEALVAA WLPGTEGQGI ADLLFGDYGF
TGKLPRTWFK SVDQLPMNVG DPHYDPLFPF DFGLTINSSQ PGFSGAEQLR DRNGRTIYLV
LSSVLSVILI HSSILA
//
