The cecropin superfamily of toxic peptides.
All sequenced peptide toxins of the cecropin, pleurocidin and dermaceptin/ceratotoxin families in the National Center for Biotechnology Information (NCBI) database as of May 2005 were identified and shown to comprise a single superfamily. The peptide sequences were multiply aligned, revealing conserved residues that may play roles in structure and function. Signature sequences were derived for each of the 3 constituent families. Phylogenetic analyses revealed the relationships of these peptides to each other, and average hydropathy/amphipathicity studies provided structural information. This study serves to characterize a large superfamily of toxic peptides that perform host defense functions in a range of animal kingdoms.
Tamang
Dorjee G
DG
Division of Biological Sciences, University of California at San Diego, La Jolla 92093-0116, USA.
Saier
Milton H
MH
D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000737:chemistry* / Q000145:classification; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000145:classification; D030562:Databases, Protein; D019143:Evolution, Molecular; D029941:Fish Proteins / Q000737:chemistry* / Q000145:classification; D019476:Insect Proteins / Q000737:chemistry* / Q000145:classification; D008969:Molecular Sequence Data; D010802:Phylogeny
D029845:Amphibian Proteins; D023181:Antimicrobial Cationic Peptides; D029941:Fish Proteins; D019476:Insect Proteins; C105851:pleurocidin; C070905:dermaseptin