This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the polyadenylation factor CPSF-73/CPSF-100 proteins. The exact function of this domain is not known.
This is the C-terminal conserved region of the pre-mRNA 3'-end-processing of the polyadenylation factor CPSF-73/CPSF-100 proteins. The exact function of this domain is not known.
Family alignment:
There are 1543 CPSF73-100_C domains in 1542 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing CPSF73-100_C domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with CPSF73-100_C domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing CPSF73-100_C domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processingendonuclease.
Nature. 2006; 444: 953-6
Display abstract
Most eukaryotic messenger RNA precursors (pre-mRNAs) undergo extensivematurational processing, including cleavage and polyadenylation at the3'-end. Despite the characterization of many proteins that are requiredfor the cleavage reaction, the identity of the endonuclease is not known.Recent analyses indicated that the 73-kDa subunit of cleavage andpolyadenylation specificity factor (CPSF-73) might be the endonuclease forthis and related reactions, although no direct data confirmed this. Herewe report the crystal structures of human CPSF-73 at 2.1 A resolution,complexed with zinc ions and a sulphate that might mimic the phosphategroup of the substrate, and the related yeast protein CPSF-100 (Ydh1) at2.5 A resolution. Both CPSF-73 and CPSF-100 contain two domains, ametallo-beta-lactamase domain and a novel beta-CASP (named formetallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain. The active siteof CPSF-73, with two zinc ions, is located at the interface of the twodomains. Purified recombinant CPSF-73 possesses RNA endonuclease activity,and mutations that disrupt zinc binding in the active site abolish thisactivity. Our studies provide the first direct experimental evidence thatCPSF-73 is the pre-mRNA 3'-end-processing endonuclease.
Links (links to other resources describing this domain)
