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. 2008 May 5;105(19):6993–6997. doi: 10.1073/pnas.0802293105

Fig. 2.

Fig. 2.

Structural analysis of cnRNAs 15 and 194. Sense and antisense strands are defined by the orientation of the 5′ caps and 3′ polyadenylation sites. Blue bars represent the 692- and 671-nt sequences originally cloned from isolated centrosomes; arrows indicate 5′ to 3′ orientation. cnRNA15 includes a 314-nt putative protein coding domain (red) with 85% identity at the amino acid level to a newly described Spisula zinc finger protein (ZFP; GenBank accession no. AB231865). The homology domain in cnRNA15 does not correspond to the C2H2 zinc-binding motif region. In addition, a 1,128-nt domain is present in the antisense strand that exhibits 40% identity (at the amino acid level) to S. purpuratus endonuclease/RVT (GenBank accession no. XP792610). An amino acid-binding domain similar to that found in glutamate receptors and other amino acid-binding proteins from a variety of species is present in the 5′ end of cnRNA194, overlapping with a cathepsin-like cysteine protease (CysP) protease domain (green) [GenBank accession nos. EU069824 (cnRNA15) and EU069825 (cnRNA194).]