Figure 4.
Multiple Alignments of VTE5 Orthologs and Dolichol Kinases.
(A) Multiple alignments were visualized and edited using GeneDoc (Nicholas et al., 1997). The residues are shaded using conserved residue shading mode set to level 4 using default settings. Similar amino acid residues conserved in all columns have dark shading. Amino acids with 100, 80, and 60% conservation are shaded as white letters on black background, white letters on dark-gray background, and black letters on light-gray background, respectively. N-terminal nonconserved amino acids encoding putative chloroplast target sequences were deleted from the alignment. Numbers above the sequence refer to amino acid positions within the Arabidopsis VTE5 sequence. Arrowhead indicates the location of vte5-1 mutation, which is predicted to cause truncation of the remaining amino acid residues. Reference numbers are as follows: At3g45040, putative Arabidopsis dolichol kinase; Arabidopsis VTE5, At5g04490; numbers starting with the prefix DQ represent accession numbers; SEC59, S. cerevisiae dolichol kinase, accession number gi|728645; Synechocystis vte5, nucleotides 3,452,461 to 3453162, accession number gi|47118304. Aa, Aquifex aeolicus VF5; Af, Archaeoglobus fulgidus; At, Arabidopsis thaliana; Av, Anabaena variabilis; Ca, Chloroflexus aurantiacus; Ct, Chlorobium tepidum; Gm, Glycine max; Np, Nostoc punctiforme; Os, Oryza sativa; Pa, Pyrococcus abyssi; Sc, Saccharomyces cerevisiae; Syn, Synechocystis sp PCC 6803; Te, Thermosynechococcus elongatus; TP, chloroplast target peptide; Zm, Zea mays.
(B) Shematic drawing of Arabidopsis VTE5 aligned to the conserved PFAM domain of cytidylyltransferases (CTP_transf_1) and dolichol kinase (SEC59).