Novel Protein Domains and Repeats in Drosophila melanogaster: Insights into Structure, Function, and Evolution

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Figure 3.Figure 3.
Figure 3.

Schematic representation, shown approximately to scale, of the domain architectures of some of the proteins containing repeats or domains that are discussed in the text. Abbreviations: AAA, ATPases associated with a variety of cellular activities; AspRS core, the catalytic portion of aspartyl tRNA synthetases; Bbox, B-box type zinc finger; C2, Protein kinase C conserved region 2 (CalB) domain; F, F-box domain; OB, oligonucleotide/oligosaccharide binding fold; PH, pleckstrin homology domain; R, RING finger domain; T, tectonin-like β-propeller repeats; UCH-1, UCH-2, Ubiquitin carboxyl-terminal hydrolases family 2 (two conserved regions); WD, β-propeller repeat with conserved Trp (W) and Asp (D) residues; ZnF_UBP, Ubiquitin carboxy-terminal hydrolase-like zinc finger; ZnF_UBR1, domain that is involved in recognition of N-end rule substrates in yeast Ubr1p. Solid vertical lines represent predicted transmembrane helices. Double forward slash lines indicate that the protein sequence is N-terminally truncated.

This Article

  1. Genome Res. 11: 1996-2008

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