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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.
Beta-Casp domain
The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains [1]. [1]. 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. (from Pfam)
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)
MBL fold metallo-hydrolase is most likely a hydrolytic enzyme; similar to Thermus thermophilus ribonuclease TTHA0252, which exhibits endoribonuclease activity towards 23S and 16S rRNA in vitro and may function in RNA degradation
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