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. 2005 Jan 20;61(Pt 2):212–215. doi: 10.1107/S174430910500062X

Figure 2.

Figure 2

Multiple alignment of the mimivirus TyrRS sequence with structural homologues and related archeal and eukaryotic sequences. j1u and n3l correspond to the PDB structures http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1j1u (Kobayashi et al., 2003 ▶) and http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1n3l (Yang et al., 2002 ▶). The accession numbers of the homologous sequences are as follow: Ehisto, Entamoeba histolytica unfinished genome (gnl|TIGR_5759, ENTER63TR); Osati, Oryza sativa putative TyrRS (Q84PX0); Atha1, Arabidopsis thaliana putative TyrsRS (Q8S9J2); Atha2, Arabidopsis thaliana putative TyrsRS (P93018); Tobac, Nicotiana tabacum putative TyrRS (P93363); Pyoeli, Plasmodium yoelii putative TyrRS (Q7RH02); CParvum, Cryptosporidium parvum putative TyrRS(Q7YYA0). Black triangles correspond to residues known to be involved in interaction with the tyrosine, green triangles correspond to residues known to be involved in interaction with the acceptor and red stars correspond to residues known to be involved in interaction with the anticodon. The multiple alignment was generated using the T-COFFEE software (Poirot et al., 2004 ▶) in order to combine structural and sequence information and was used through the CaspR procedure to generate homology-based models of the mimivirus structure.