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Fig. 2 | Journal of Genetic Engineering and Biotechnology

Fig. 2

From: Molecular characterization of a novel β-defensin isoform from the red-toothed trigger fish, Odonus niger (Ruppel, 1836)

Fig. 2

a cDNA (192 bp) and deduced amino acid (63 aa) sequences of β-defensin from Odonus niger. The blue boxed amino acid sequences (20 aa) denote the signal peptide region with cleavage site predicted in between the Gly20-N21 residues with SignalP-5.0. The remaining 43 aa residue of mature peptide sequence is in yellow shade. All positively charged residues are shown in bold, and the cysteine residues are double-underlined. ‘*’ denotes termination. b An illustration of the SMART and Pfam identified β-defensin domain is shown in green shade (C30–C59) within which three predicted disulfide bonds of the pattern C1–C5, C2–C4, and C3–C6 are shown

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