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. 2019 Nov 14;82(1):47–55. doi: 10.1292/jvms.18-0125

Fig. 2.

Fig. 2.

Multiple sequence alignment of CagC3 in comparison with C3 sequences of other vertebrates. Carp (Cyprinus carpio C3-H1, accession no. BAA36619.1), zebrafish (Danio rerio C3a, NP_571317.1), mouse (Mus musculus C3, NP_033908.2) and human (Homo sapiens C3, AAA85332.1) C3 protein sequences were compared using ClustalW (v. 2.1) and MEGA 5 software. Amino acid numbering is indicated on the right. Identical residues are indicated by black shading and with an asterisk (*). Conserved and semi-conserved residues are indicated by semicolons (:) and periods (.), respectively. Names and boundaries of protein domains are shown above the sequences. Characteristic domains and motifs are highlighted below the sequences: the ANATO domain has six canonical cysteine residues at conserved positions (solid black line); the thioester domain (●); the RKRR cleavage site of the alpha and beta chains (☆).