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. 2023 Dec 23;22(1):12. doi: 10.3390/md22010012

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© 2023 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Chitinases. (A) Alignment of the amino acid sequences of the putative Exaiptasia pallida Chitotriosidase-1-like (XP_020909717.1) with chitinases from rats (Uni-ProtKB: CHIA_RAT), sea anemones (REFSEQ: XP_020902061.1) and humans (GenBank: AAM57182.1, AAE83140.1 y AAE83141.1). The magenta background shows the region covered by the tryptic peptides obtained from the proteomes of A. dowii and L. neglecta. The region corresponding to the signal peptide is underlined and the region of the mature protein is indicated in bold. The residues that make up the active and chitooligosaccharide binding sites are shaded black and highlighted with white letters. Cysteines involved in disulfide bond formation are underlined. (B) Structure models of chitinase: XP_020909717.1 is shown in green, XP_02092061.1 is in red, AAM57182.1 is yellow, AAE83140.1 is represented in gray, AAE83141.1 is blue, and CHIA_RAT is in purple. The comparison of the Cα chains presented RMSD values that oscillate between 0.127 and 0.616.