Sanitizing with quality score

<p>Publicly available RNA-Seq data (SRR100067) from wild type Neurospora crassa 74-OR23-1VA were obtained from the NCBI, http://www.ncbi.nlm.nih.gov/Traces/sra to generate these datasets</p

DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways-0

<p><b>Copyright information:</b></p><p>Taken from "DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways"</p><p>BMC Structural Biology 2006;6():1-1.</p><p>Published online 5 Jan 2006</p><p>PMCID:PMC1360078.</p><p></p> eukaryotic genomes analysed to date, including the single celled parasite , in which it is very much reduced in size. In vertebrates and insects the protein includes a long C-terminal extension containing p53 and Rb-interaction domains in human and mouse. A short form consisting of the DWNN domain and a poorly conserved C-terminal tail is also found in vertebrates

DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways-4

<p><b>Copyright information:</b></p><p>Taken from "DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways"</p><p>BMC Structural Biology 2006;6():1-1.</p><p>Published online 5 Jan 2006</p><p>PMCID:PMC1360078.</p><p></p>nge (

DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways-1

<p><b>Copyright information:</b></p><p>Taken from "DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways"</p><p>BMC Structural Biology 2006;6():1-1.</p><p>Published online 5 Jan 2006</p><p>PMCID:PMC1360078.</p><p></p>t single copy number, but not in prokaryotes. The alignment was performed using ClustalX [39] and the diagram produced using Pfaat [49]

DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways-2

<p><b>Copyright information:</b></p><p>Taken from "DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways"</p><p>BMC Structural Biology 2006;6():1-1.</p><p>Published online 5 Jan 2006</p><p>PMCID:PMC1360078.</p><p></p>condary structural elements are derived from the final family of structures. Coupling constants were extracted from a N-HMQC-J spectrum. Half-circles correspond to J< 4 Hz; filled circles correspond to J> 8 Hz, except in the case of residues 56-7, which have Jvalues of 7.4 and 7.7 Hz respectively. These residues form part of strand β, which is the least stable of the five strands making up the main β-sheet. The presence of a β-sheet comprised of strands βand β, which does not occur in ubiquitin, is confirmed by large values of J, negative Cshifts and αN(i,i+1) NOE's. The diagram was generated using CYANA [45]

DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways-3

<p><b>Copyright information:</b></p><p>Taken from "DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways"</p><p>BMC Structural Biology 2006;6():1-1.</p><p>Published online 5 Jan 2006</p><p>PMCID:PMC1360078.</p><p></p>and secondary structure. The backbone adopts a ubiquitin-like β-grasp fold in which the central α-helix packs against a five-stranded β-sheet comprised of strands β, β, β, βand β. Unlike ubiquitin, DWNN contains an additional double-stranded β-sheet at the N-terminal end of the central α-helix, comprising strands βand β. (C) Superposition of the backbone traces of the DWNN domain (in blue) and ubiquitin (1UBI, in yellow). The RMSD over structurally aligned regions between the two structures is 1.88 Å. (D) Structural alignment of the primary sequences of DWNN and ubiquitin, determined using the Dali server. The structurally equivalent regions comprise the following residues of DWNN: 2–9, 11–20, 22–40, 44–50, 53–57, 59–64, 66–75. Molecular fitting, calculation of RMSD's and generation of figures were performed using MOLMOL [26]