Fig. 1: Conserved domain and sequence motifs in the DMSP lyase (DL) protein. | ISME Communications

Fig. 1: Conserved domain and sequence motifs in the DMSP lyase (DL) protein.

From: Phylogeny and biogeography of the algal DMS-releasing enzyme in the global ocean

Fig. 1: Conserved domain and sequence motifs in the DMSP lyase (DL) protein.

A The DL enzyme Alma1 cleaves DMSP to produce DMS and acrylate. It has an Asp/Glu/Hydantoin conserved domain, which contains ten unique amino acid motifs. The motifs are numbered according to their order in the sequence and are colored according to their E-value score. The E-value represents how the sequence is significantly shared between 151 DLHs and also discriminant from 917 bacterial racemase domains. B The sequence logos of the ten identified conserved motifs, numbered as in (A). *According to the E. huxleyi Alma1 sequence [1].

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