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Fig. 2. neverland is conserved among several animal species. (A) Predicted polypeptides that are produced from nvd-Bm (Bombyx mori) (GenBank Accession Number AB232986) and its closest relatives from Drosophila melanogaster (AB232987), Anopheles gambiae (XP_309236.1), Caenorhabditis elegans (NP_505629), Ciona intestinalis (EST clones cicl031b24 and cicl077j15 from the Ciona cDNA database; http://ghost.zool.kyoto-u.ac.jp/cgi-bin/getblast1.cgi), Danio rerio (NP_001002612), Gallus gallus (XP_425346), Rhodococcus erythropolis (kshA gene, AAL96829) and Pseudomonas fluorescens (prnD gene, U74493). These polypeptides share a Rieske domain (dark gray) and a highly conserved domain in the C-terminal region (light gray). The bars above each domain indicate the positions of the [2Fe-2S] binding motif (C-X-H-X_16-17-C-X₂-H) and the non-heme iron-binding motif [Fe(II); E-X₃-D-X₂-H-X₄-H]. Percentages represent amino acid identities between each domain of nvd-Bm and that of others. Also indicated are the total numbers of residues for individual proteins. The Anopheles and Ciona orthologs are incompletely predicted on both ends. A black box indicates the transmembrane domain predicted by TMHMM software (http://www.cbs.dtu.dk/services/TMHMM/). (B) Sequence alignment of the Rieske motif and the non-heme iron-binding motif of Nvd-Bm with its closest relatives. Identical residues in all nine species are white on black, while identical residues in five or more species are boxed. The evolutionally conserved amino acids of the Rieske domain and non-heme iron binding motif are indicated above the alignment.

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