The cwf21 family is involved in mRNA splicing. It has been isolated as a subcomplex of the splicosome in Schizosaccharomyces pombe . The function of the cwf21 domain is to bind directly to the spliceosomal protein Prp8. Mutations in the cwf21 domain prevent Prp8 from binding . The structure of this domain has recently been solved which shows this domain to be composed of two alpha helices.
The cwf21 domain is found in proteins involved in mRNA splicing. Proteins containing this domain have been isolated as a subcomplex of the splicosome in Schizosaccharomyces pombe (Fission yeast) [PUBMED:11884590]. In yeast, this domain binds the protein Prp8p [PUBMED:19854871], a large and highly conserved U5 snRNP protein which has been proposed as a protein cofactor at the spliceosomal catalytic centre [PUBMED:11017191].
Ohi MD, Link AJ, Ren L, Jennings JL, McDonald WH, Gould KL; , Mol Cell Biol 2002;22:2011-2024.: Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs. PUBMED:11884590 EPMC:11884590 .
Grainger RJ, Barrass JD, Jacquier A, Rain JC, Beggs JD;, RNA. 2009; [Epub ahead of print]: Physical and genetic interactions of yeast Cwc21p, an ortholog of human SRm300/SRRM2, suggest a role at the catalytic center of the spliceosome. PUBMED:19854871 EPMC:19854871.