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. Author manuscript; available in PMC: 2010 May 29.
Published in final edited form as: Cell. 2009 May 29;137(5):938–948. doi: 10.1016/j.cell.2009.03.043

Figure 1. Alignment of RhoBTB3 with RhoBTB 1 and 2 and RhoA.

Figure 1

(A) Amino acid residues are listed at the top; numbers at left indicate RhoBTB1, 2 or 3. Each of the proteins has an N-terminal Rho domain (red) and at least one intact BTB domain (blue). Because RhoBTB has a single ancestor closest to RhoBTB1 and 2, the conserved domain database identified these as “RhoBTB” domains, a subset of Rho domains (Marchler-Bauer et al., 2007). RhoBTB3 is unique with a C-terminal CAAX prenylation motif (CLVM shown). (B) Sequence alignment of RhoBTB3’s Rho domain with RhoA and the Rho domain of RhoBTB2. Canonical features of typical GTPases are noted (G1 P-loop, G2, G3 and G4). Arrow points to Asn138. In all GTPases, this residue is Asp and confers specificity for guanosine.