Fig. 7. Peculiarities in the anticodon-binding domain of AspRS-2 from T.thermophilus as revealed by sequence comparison with other AspRSs. (T.t.2, T.t.1) AspRSs from T.thermophilus, (D.r.) D.radiodurans and (Euka., Arch., Bact.) consensus sequences from eukarya, archaea and eubacteria. (–) Non-conserved residues; semi-conserved residues with φ, h, a, b, s representing, respectively, aromatic, hydrophobic, acid, basic and small (Gly, Ala, Ser) side chains; (*) missing amino acids. Residues belonging to β-strands (S1, S2, S3, S4 and S5) of the OB-fold are on a grey background. Lα/Hα and L1 regions are boxed. Amino acids in AspRS-1 that contact the three anticodon identity determinants of tRNA^Asp (G34, U35 and C36) are in bold. Notice the differences in length and sequence in L1.