Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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CPSF73-100_C

SMART accession number:	SM01098
Description:	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.
Interpro abstract (IPR021718):	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:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 169 CPSF73-100_C domains in 169 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a CPSF73-100_C domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with CPSF73-100_C domain is also avaliable.

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  Go to specific node: Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Mandel CR et al.
  • 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)

• PFAM	CPSF73-100_C
  INTERPRO	IPR021718

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