LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Family |
| Description | This family consists of ribonuclease III (RNase III). This ubiquitous enzyme specifically cleaves double-stranded rRNA and is found in all bacteria and eukaryotes [ ]. In bacteria its main role is the processing of pre-rRNAs, where the large precursor ribosomal RNA molecules are cleaved at specific sites to produce the immediate precursors of the functional molecules. RNase III also functions in the maturation and degradation of mRNAs, and the maturation of tRNAs. In some organisms (eg. Escherichia coli) cells are viable without this enzyme, though they are impeded in growth, but in others (eg. B. subtilis and M. genitalium) this enzyme is essential.The bacterial RNase III enzymes so far characterised are homodimers with a molecular mass of ~50kDa [ , ]. The endonuclease domain is located within the N-terminal two-thirds of the protein, containing several α-helices, but no β-strands. The double-stranded RNA binding domain is found at the C-terminal third of the protein, forming the α-β(3)-α fold common to dsRNA-binding proteins. A signature box of 11 conserved amino acids found in the N-terminal region of RNase III may contain the active site, though this has not been proven. |
| Short Name | RNase_III |
