ID A0A0D9V699_9ORYZ Unreviewed; 1047 AA.
AC A0A0D9V699;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:LPERR01G28050.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR01G28050.1, 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:LPERR01G28050.1, 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:LPERR01G28050.1}
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; A0A0D9V699; -.
DR STRING; 77586.A0A0D9V699; -.
DR EnsemblPlants; LPERR01G28050.1; LPERR01G28050.1; LPERR01G28050.
DR Gramene; LPERR01G28050.1; LPERR01G28050.1; LPERR01G28050.
DR eggNOG; ENOG502QQ55; Eukaryota.
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 1047 AA; 114200 MW; E0324F6950DACFDA 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 YSVQAGINAG
IDMVMVPYHY TDYINNVTSL VKKGVISMSR IDDAVRRILR VKFTMGLFES PLADLSFSDQ
LGKKEHRELA REAVRKSLVL LKNGNSPNQQ FLPLPKKARS ILVAGSHADN LGYQCGGWSI
KWFAASGDIT VGTTILDAIK STVADSTHVV YSENPDESFM KENDFSFAIV VVGEPPYAET
VGDSTELTIL DPGTDTIRTV CSTVKCAVVI ISGRPVVIEP YLPMMEALVA AWLPGTEGQG
IADLLFGDYG FTGKLPRTWF KSVDQLPMNV GDPHYDPLFP FDFGLTINSS QPGFSGAEQL
RDRNGRTIYL VLSSVLSVIL IHSSILA
//
