AcT-2: A Novel Myotropic and Antimicrobial Type 2 Tryptophyllin from the Skin Secretion of the Central American Red-Eyed Leaf Frog, Agalychnis callidryas
Comparison of the primary structure of AcT-2 with those of similar peptides. PAF26 and combi-1 are synthetic antifungal peptides isolated from combinatorial peptide libraries [12, 13]. Prophenin-2-like is a region of an antimicrobial polypeptide, cathelicidin, sequenced from a genomic DNA template of the killer whale (Orcinus orca) (accession no. XP004284013). Conserved amino acid residues are shaded black and consensus residues are shaded grey (a). Nucleotide and translated open-reading frame amino acid sequence of a cloned cDNA encoding the biosynthetic precursor of AcT-2. The putative signal peptide is double-underlined, the mature peptide is single-underlined and the stop codon is indicated by an asterisk (b). Alignments of complete open-reading frame amino acid sequences of AcT-2 precursor-encoding cDNA with the two top hits obtained following BLAST analysis using the NCBI portal. PdT-1 and PdT-2 represent Pachymedusa dacnicolor tryptophyllin-1 and -2, respectively. Conserved amino acids are shaded black and consensus amino acids are shaded grey. Gaps have been inserted to maximize alignments. (1) Putative signal peptide domain. (2) Acidic spacer peptide domain. (3) Mature peptide domain. (4) C-terminal processing site (c).
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