Research Article
α-Actinin TvACTN3 of Trichomonas vaginalis Is an RNA-Binding Protein That Could Participate in Its Posttranscriptional Iron Regulatory Mechanism
Table 3
Putative motifs present in tvactn3 that may be involved in DNA-RNA interactions.
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The protein sequence of tvactn3 was used to search in the SMART 7 program to identify the presence of DNA-RNA binding putative domains in the aa sequence. The computational program used for this analysis presented the aa in a single word code. The other codes mean the following: (−) aa negatively charged: D or E; (*) aa S or T; (l) Aliphatic aa: I, L, V; (+) aa positive charged; (t) A, G, S aa; (a) aa with aromatic group: F, H, W, Y; (c) charged aa: D, E, H, K, R; (s) small aa: A, C, D, G, N, P, S, T, V; (p) polar aa: C, D, E, H, K, N, Q, R, S, T; (b) Big aa: E, F, H, I, K, L, M, Q, R, W, Y; (h) Hydrophobic aa: A, C, F, G, H, I, L, M, T, V, W, Y. bA PSI-BLAST search using the complete tvactn3 sequence (residues 1–1129) of T. vaginalis and enable us to identify each of the DNA-RNA binding domains sequences (BRIGHT/ARID, B5, LA, Pumilio-Binding, and KH domains) present in the DII of tvactn3 shown in Figure 8(d). These aa sequences showed a 60% similitude with the consensus sequences of these motifs by multiple alignments. |