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Database: UniProt
Entry: R0HII2_9BRAS
LinkDB: R0HII2_9BRAS
Original site: R0HII2_9BRAS 
ID   R0HII2_9BRAS            Unreviewed;       609 AA.
AC   R0HII2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=CARUB_v10016864mg {ECO:0000313|EMBL:EOA23658.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA23658.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(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, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; KB870809; EOA23658.1; -; Genomic_DNA.
DR   RefSeq; XP_006290760.1; XM_006290698.1.
DR   AlphaFoldDB; R0HII2; -.
DR   STRING; 81985.R0HII2; -.
DR   GeneID; 17885531; -.
DR   KEGG; crb:17885531; -.
DR   eggNOG; ENOG502QQ55; Eukaryota.
DR   OrthoDB; 1208905at2759; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
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   InterPro; IPR019800; Glyco_hydro_3_AS.
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:SF33; BETA-D-GLUCAN EXOHYDROLASE-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          30..358
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
FT   DOMAIN          395..604
FT                   /note="Glycoside hydrolase family 3 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01915"
SQ   SEQUENCE   609 AA;  66378 MW;  3D1C89FF2A6E97C5 CRC64;
     MVVKDESSCV YKNRDAPVEA RVKDLLSRMT LPEKIGQMTQ IERNVASPVA ITDSFIGSVL
     NAGGSAPFED AKSSDWADMI DGFQRSALAS RLGIPIIYGT DAVHGNNNVY GATVFPHNIG
     LGATRDADLV RRIGAATALE VRASGVHWAF SPCVAVLRDP RWGRCYESYG EDPGLVSEMT
     SLVSGLQGVP PEEHPNGYPF VAGRNNVVAC AKHFVGDGGT DKGINEGNTI ASYEDLERIH
     ITPYLKCLSQ GVSTVMASYS SWNGTQLHAD RFLLTEILKD KLGFKGFLVS DWEGLDRLSK
     PQGSNYRNCI KTSVNAGIDM VMVPLKYDQF IQDMTDLVES GEIPMDRVND AVERILRVKF
     VAGLFEHPLT DRSLLRTVGC KEHRELAQEA VRKSLVLLKN GKNADKPFLP LDRKAKRILV
     TGTHADDLGY QCGGWTKTWF GLSGRITIGT TLLDAIKAVV GDKTEVIYEK NPSKETLASS
     EGFSYAIVAV GEPPYAEATG DNSELTIPFN GSDIVTAVAE KIPTLVVLIS GRPVVLEQRV
     LEKTDALVAA WLPGTEGQGM ADVIFGDYDF EGKLPVSWFK RVEHLPLDAN ANSYDPLFPF
     GFSLNSKPL
//
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