Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
ribonuclease J1
Ribonuclease J1, as the term is used in Staphylococcus aureus, is one of two RNase J paralogs that are about 40 percent identical.
Ribonuclease J C-terminal domain
This domain is found at the C-terminus of Ribonuclease J proteins. Its function is unknown, but deletion of this domain causes dissociation to monomers [2]. [1]. 21893286. Molecular basis for the recognition and cleavage of RNA by the. bifunctional 5'-3' exo/endoribonuclease RNase J.. Dorleans A, Li de la Sierra-Gallay I, Piton J, Zig L, Gilet L,. Putzer H, Condon C;. Structure. 2011;19:1252-1261.. [2]. 18204464. Structural insights into the dual activity of RNase J.. Li de la Sierra-Gallay I, Zig L, Jamalli A, Putzer H;. Nat Struct Mol Biol. 2008;15:206-212. (from Pfam)
Ribonuclease J, beta-CASP domain
MBL fold metallo-hydrolase
The MBL fold superfamily includes the metallo-beta-lactamases (class B beta-lactamases), but includes also a much larger family of hydrolases that are not beta-lactamases at all. See also the related family PF00753.
MBL fold metallo-hydrolase RNA specificity domain-containing protein
The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in Pfam:PF00753 and are common to all metallo-beta-lactamases. This, the fifth motif [1], appears to be specific to Zn-dependent metallohydrolases such as ribonuclease J 2 [4] which are involved in the processing of mRNA [2,3]. This domain adds essential structural elements to the CASP-domain and is unique to RNA/DNA-processing nucleases, showing that they are pre-mRNA 3'-end-processing endonucleases [2,3,4]. [1]. 12177301. Metallo-beta-lactamase fold within nucleic acids processing. enzymes: the beta-CASP family.. Callebaut I, Moshous D, Mornon JP, de Villartay JP;. Nucleic Acids Res 2002;30:3592-3601.. [2]. 17128255. Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing. endonuclease.. Mandel CR, Kaneko S, Zhang H, Gebauer D, Vethantham V, Manley. JL, Tong L;. Nature. 2006;444:953-956.. [3]. 20544974. Crystal structure of an archaeal cleavage and polyadenylation. specificity factor subunit from Pyrococcus horikoshii.. Nishida Y, Ishikawa H, Baba S, Nakagawa N, Kuramitsu S, Masui R;. Proteins. 2010;78:2395-2398.. [4]. 21764917. Characterization of components of the Staphylococcus aureus mRNA. degradosome holoenzyme-like complex.. Roux CM, DeMuth JP, Dunman PM;. J Bacteriol. 2011;193:5520-5526. (from Pfam)
ribonuclease J
ribonuclease J plays a key part in RNA processing and in RNA degradation; it can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on