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Multiple alignment showed that the deduced LhSorP5CS amino acid sequence exhibited high homology with other P5CS proteins from plants, such as MaAAAP5CS (83%), TaP5CS (77%), OsP5CS1 (79%), and ZmP5CS (79%).
The multiple alignment showed high sequence similarity to other thrombin-like enzymes from snake venoms.
Multiple alignment showed higher identity and similarity between the C termini of paralogs, which contain the functional portion of the proteins.
Multiple alignment showed a premature stop codon, which prevents the encoding of the conserved cysteine residue at the E2 active site, and an intron that is spliced in E2 homologues, but not in GhGDRP85.
Multiple alignment showed that the highly conserved DBD is located close to the N-terminal in all the cotton Hsf proteins (Table 2, Figure 1), and comprises 83, 94, 102 or 105 amino acid residues.
In addition, a multiple alignment showed that intron 2 from Calliphorinae species, such as T. calliphoroides, A. grahami, C. vicina, and C. lata, differed from those of the Luciliinae species, such as H. ligurriens, L. caesar, L. illustris, L. ampullaceal, and L. sericata (Table 2).
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The multiple alignment shown in Fig. S2 for the β-barrel domains was used to derive average hydropathy, amphipathicity and similarity plots (Fig. 5).
In each position of the family, multiple alignment shows an average identity of amino acids of ∼30%.
Examination of sequences in the multiple alignment shows not only that Cys tends to occur every third residue in the carboxyl-terminal region, but also that differences between closely related sequences commonly feature tripeptide indels.
Multiple alignments showed that maize ZmNF-Y family proteins had conserved regions and relatively variable N-terminal or C-terminal domains.
All the sequences from each of the cluster when subjected to multiple alignments showed that the strains were fairly similar over a large region.
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