Not all primate RanBP2 proteins are the same.

<p><b>A</b>) A domain diagram of RanBP2 is shown. TPR, tetratricopeptide; RBD, Ran binding domain; Cyp, Cyclophilin. <b>B</b>) Protein schematic of TRIM-fusion constructs showing the tripartite RING/B-Box/Coiled-coil (RBCC) domain fused to a cyclophilin domain. <b>C)</b> CRFK cell lines transduced to stably express different TRIM-RanCyps (bottom) were infected with VSV-G pseudotyped HIV-1, FIV, or NB-MLV, all encoding a GFP reporter. The percentage of cells infected in each sample was normalized to the empty vector control. A western blot detecting HA-tagged TRIM-RanCyp constructs is shown along with a β-actin loading control. Infections were performed in triplicate and error bars represent twice the standard error of the mean. <b>D)</b> Partial protein alignment of the RanCyp domain from primates in C. Here, residue coordinates refer to the coordinates of the human RanCyp domain (see exact numbering scheme in <b><a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1006906#ppat.1006906.s002" target="_blank">S1 Fig</a></b>; 3060 needs to be added to these numbers to convert them to the residue position in full-length human RanBP2). Asterisks (*) indicate conserved residues. Red text indicates species-specific differences at non-conserved sites.</p>