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. Author manuscript; available in PMC: 2022 Apr 21.
Published in final edited form as: FEMS Microbiol Lett. 2008 Dec;289(2):202–209. doi: 10.1111/j.1574-6968.2008.01397.x

Fig. 3.

Fig. 3.

(a) RBPs and lytic conversion lipoprotein precursor (Llps) modules of four T5-like viruses. White and black arrows are RBP and Llp proteins, respectively. Hypothetical proteins of BF23 and T5 are reported to be similar to each other (Mondigler et al., 2006), but those of EPS7 and H8 do not contain significant homology with that of T5. (b) CLUSTAL W analysis of RBPs of T5-like viruses, BF23, EPS7, T5 and H8. Boxes show five conserved regions (C1–C5) and two variable regions (V1 and V2) (Mondigler et al., 1996), while the dotted boxes in T5 indicate regions that are reported to be essential for T5 binding to the host receptor (Mondigler et al., 1996). (c) CLUSTAL W alignment of lytic conversion lipoprotein precursors from BF23, EPS7 and T5.