Skip to main content
. Author manuscript; available in PMC: 2013 Jul 24.
Published in final edited form as: Insect Mol Biol. 2008 Sep;17(5):545–552. doi: 10.1111/j.1365-2583.2008.00823.x

Figure 2.

Figure 2

Conservation of mosquito and other dipteran Nos and Osk protein domains. (A) Alignment of the amino acids composing the zinc-finger domain (pfam05741, zf-nanos, Nanos RNA binding domain) of insect Nos proteins. Conserved cysteine and histidine amino acid residues that form two zinc-finger motifs are indicated by asterisks. Amino acids conserved among all sequences are shaded in black. Amino acid positions are indicated with numerals. Abbreviations (Genbank accession numbers are referenced in parentheses): AngaNos, Anopheles gambiae Nanos protein (AAS93544); AnstNos, Anopheles stephensi Nanos protein (AAS93543); AeaeNos, Aedes aegypti Nanos protein (AAS93542); CxquNos, Culex quinquefasciatus Nanos protein (EU517696); DmelNos, Drosophila melanogaster Nanos protein (AAA28715); DsimNos, Drosophila simulans Nanos protein (AAF68506); MdomNos, Musca domestica Nanos protein (AAA87461); CsamNos, Chironomus samoensis Nanos protein (AAA87459). (B) Sequence alignment of the C-terminal regions of predicted mosquito and Drosophila Osk proteins. Amino acids conserved in sequence in all, five-of-six and four-of-six species are shaded in black, dark grey and light grey, respectively. Amino acid positions are indicated with numerals. Abbreviations (Genbank accession numbers are referenced in parentheses): AngaOsk, An. gambiae Oskar protein (ABC54566); AeaeOsk, Ae. agypti Oskar protein (ABC41128); Cxqu Osk, Cx. quinquefasciatus Oskar protein (EU517695); DmelOsk, D. melanogaster Oskar isoform A protein (AAF54306); DvirOsk, Drosophila virilis Oskar protein (AAA28426); DimmOsk, Drosophila immigrans Oskar protein (ABH12272).