Drosophila melanogaster amino acid sequences

Figure 2. Histone H2A variants from yeast Saccharomyces cerevisiae S.c.), fruit fly Drosophila melanogaster D.m ), and human Homo sapiens H.s.). Two conserved domains distinguish H2A.Z-relatives (boxed regions amino acid sequences in the top). H2A.X possesses a conserved C-terminal stretch of four amino acids. The serine (red) becomes phosphorylated at sites of DNA damage. H2A ( Barr body-deficient ) and marcoH2A are present in mammals...

Fig. 3. Comparison of the deduced amino acid sequence of the consensus element Loa from the Hawaiian Drosophila (D. silvestris, lower line) and the ribosomal insertion sequence, Rl, element from D. melanogaster (upper line). The amino acids above the sequences at that site are found in the putative reverse transcriptase of at least five of six non-LTR retrotransposons.23 The amino acids below the sequences are invariant in the reverse transcriptase of retroviruses.2 ...

Fig. 1. Elongation factor distance-matrix phylogenetic trees inferred from amino-acid sequence identities. Top phylogenetic tree inferred from EF-lcn/(EF-Tu) sequences. Bottom phylogenetic tree inferred from EF-2/(EF-G) sequences. Abbreviations Egr, Euglena gracilis See, Saccharomyces cerevisiae Asa, Artemia salina Dme, Drosophila melanogaster Hsa, Homo sapiens Eco, Escherichia coli Mlu, Micrococcus luteus Tma, Thermotoga maritima.

Rep and Cro are bacteriophage 434 proteins Lam Rep and Cro are bacteriophage proteins CAP, Irp Rep, and Lac Rep are catabolite activator protein, Trp repressor, and fac repressor oiE. coli, respectively. Antpis the homeodomain protein of the Antennapedia gene of the fruit fly Drosophila melanogaster. The numbers in each sequence indicate the location of the HTH within the amino acid sequences of the various polypeptides. 

Proteins in this family are highly acidic (pi 5), and have molecular weights between 13 and 17 kDa (110-150 amino acids in length). There is considerable amino acid sequence similarity between PBPs and OBPs of the same moth species (50-60%), but little similarity with OBPs from Drosophila melanogaster and other non-lepidopteran species. OBPs and PBPs have six highly conserved cysteine residues, which form three interlocked disulfide bridges (with the pattern first with... 

Fig. 3. Alignment of partial PCNA amino acid sequences from various model eukaryotic organisms. Shaded residues match the consensus. Sc, Saccharomyces cerevisiae, Sp, Schizosaccharomyces pombe. Dm, Drosophila melanogaster, Ce, Caenorhabditis elegans At, Arabidopsis thaliana Mm, Mus musculus Hs, Homo sapiens. Lysl27 and Lysl64 residues of S. cerevisiae (indicated with arrows) are modified by SUMO only, or Ub and SUMO, respectively.

Figure 2. Amino acid sequence of the sex peptides of Drosophila melanogaster (Drm-SP-1) and D. sechellia (Drs-SP-1) (adapted from 41). The isoleucines marked with an are tentative assignments (20, 43).

Fig. 1 Blocks of multiple sequence alignment of protein sequences of carboxypeptidases from B. taurus, Mus musculus, Rattus norvegicus, Neurospora crassa, Schizosaccharomyces pombe, Drosophila melanogaster, and Homo sapiens along with protein sequence from H. pylori (Uniprot accession code HPAG1 0372 from strain HPAG1). Numbers on the top correspond to amino acid residue number of the carboxypeptidase enzyme from B. taurus. Gray vertical columns indicate conserved residues. Amino acid residues corresponding to Glu-182 and His-306, which coordinate to zinc, are conserved, whereas another Zn-coordinating amino acid residue corresponding to His-179 is substituted by Gin in the Helicobacter sequence. Functionally important residues corresponding to Arg-237 are also conserved...

Figure 2. Comparisons of the primary sequences of EcRs and USPs, Numbers in boxes show the percentage amino acid identity in each region between Chilo suppressalis and Drosophila melanogaster,...

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