RNB |
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| SMART accession number: | SM00955
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| Description: |
This domain is the catalytic domain of ribonuclease II.(PUBMED:16806266) |
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| Interpro abstract (IPR001900): |
This entry represents the catalytic domain of ribonuclease II [(PUBMED:16806266)]. It includes characterised and related sequences to exoribonuclease II (RNase II) and ribonuclease R, a bacterial 3' --> 5' exoribonuclease homologous to RNase II [(PUBMED:11948193),(PUBMED:15604703),(PUBMED:9829834)].
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| GO function: | ribonuclease activity (GO:0004540), RNA binding (GO:0003723) |
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| Family alignment: |
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There are 2611
RNB domains in 2610 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Cellular role (predicted cellular role)
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Cellular role: metabolism
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Amblar M, Barbas A, Fialho AM, Arraiano CM
- Characterization of the functional domains of Escherichia coli RNase II.
- J Mol Biol. 2006; 360: 921-33
- Display abstract
RNase II is a single-stranded-specific 3'-exoribonuclease that degradesRNA generating 5'-mononucleotides. This enzyme is the prototype of anubiquitous family of enzymes that are crucial in RNA metabolism and sharea similar domain organization. By sequence prediction, three differentdomains have been assigned to the Escherichia coli RNase II: twoRNA-binding domains at each end of the protein (CSD and S1), and a centralRNB catalytic domain. In this work we have performed a functionalcharacterization of these domains in order to address their role in theactivity of RNase II. We have constructed a large set of RNase IItruncated proteins and compared them to the wild-type regarding theirexoribonucleolytic activity and RNA-binding ability. The dissociationconstants were determined using different single- or double-strandedsubstrates. The results obtained revealed that S1 is the most importantdomain in the establishment of stable RNA-protein complexes, and itselimination results in a drastic reduction on RNA-binding ability. Inaddition, we also demonstrate that the N-terminal CSD plays a veryspecific role in RNase II, preventing a tight binding of the enzyme tosingle-stranded poly(A) chains. Moreover, the biochemical results obtainedwith RNB mutant that lacks both putative RNA-binding domains, revealed thepresence of an additional region involved in RNA binding. Such region, wasidentified by sequence analysis and secondary structure prediction as athird putative RNA-binding domain located at the N-terminal part of RNBcatalytic domain.
- Structure (3D structures containing this domain)
3D Structures of RNB domains in PDB
| PDB code | Main view | Title | | 2id0 |  | Escherichia coli rnase ii |
| 2ix0 |  | Rnase ii |
| 2ix1 |  | Rnase ii d209n mutant |
| 2r7d |  | Crystal structure of ribonuclease ii family protein from deinococcus radiodurans, triclinic crystal form. northeast structural genomics target drr63 |
| 2r7f |  | Crystal structure of ribonuclease ii family protein from deinococcus radiodurans, hexagonal crystal form. northeast structural genomics target drr63 |
| 2vnu |  | Crystal structure of sc rrp44 |
| 2wp8 |  | Yeast rrp44 nuclease |
- Links (links to other resources describing this domain)
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