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. 2013 Apr;87(7):3915–3929. doi: 10.1128/JVI.03418-12

Fig 1.

Fig 1

Polypeptide sequences of ORF67 and ORF69 and mutations made in these proteins. Shown are the amino acid sequences of KSHV ORF67 and ORF69 (strain BCBL-1 BAC36) (59). The in-frame deletions made are highlighted by black boxes, and the positions of the polypeptide truncation mutations are indicated by the arrows (T240 and T264; truncations after amino acids 239 and 263, respectively). The transmembrane domain residues of ORF67 predicted using MacVector are shown in bold. Underlined residues are those that are conserved in the gammaherpesviruses (KSHV, EBV, rhesus rhadinovirus, murine herpesvirus 68, and herpesvirus saimiri). Residues that are completely conserved in all human herpesvirus proteins that are located close to or within the in-frame deletions are in red. The amphipathic alpha-helix in ORF67 predicted by Milbradt et al. (29) is marked by a purple box, as is an alpha-helix in the N terminus of ORF69 that was determined using MacVector software. The arginine-rich region in the N terminus of ORF69, which may contain a nuclear localization signal (NLS), is shown in a green box.