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The Immunoreactive Exo-1,3-β-Glucanase from the Pathogenic Oomycete Pythium insidiosum Is Temperature Regulated and Exhibits Glycoside Hydrolase Activity

Fig 2

Protein structure of Exo1 and six transcriptome-derived homologous proteins.

Protein domains of Exo1 and homologous proteins (UN05080, UN00475, UN03240, UN01457, UN24957 and UN22794; Table 3) were predicted by SignalP, TMHMM, and NCBI’s conserved domain search programs (Methods). The DOG program was used to draw protein structures. Numbers indicate the first and last amino acid positions of each protein. Detailed characteristics of the homologous proteins are shown in Table 3. (Symbols: A, Peptide-A; B, Peptide-B; C/1, Peptide-C (the first half portion); C/2, Peptide-C (the second half portion); SP, signal peptide; BglC, BglC domain; X8, X8 domain; and TM, transmembrane region; The grey regions are sequences that do not match any protein domain defined by the NCBI’s conserved domain search program).

Fig 2

doi: https://doi.org/10.1371/journal.pone.0135239.g002