Figure 2
Sequence conservation between the C-terminal halves of fungal and non-fungal eukaryotic tRNase ZLs. Multiple sequence alignment of the C-terminal halves of representative fungal and non-fungal eukaryotic tRNase ZLs. Fungal tRNase ZLs are from A. gossypii (AgoTrz1), S. cerevisiae (SceTrz1) [19], C. albicans (CalTrz1), Yarrowia lipolytica (YliTrz1), A. nidulans (AniTrz1), Coccidioides immitis (CimTrz1), Sclerotinia sclerotiorum (SscTrz1), Pyrenophora tritici-repentis (Ptrtrz1), N. crassa (NcrTrz1), Fusarium graminearum (FgrTrz1), S. pombe (SpoTrz1 and SpoTrz2) [14], Cryptococcus neoformans (CneTrz1), M. globosa (MglTrz1), Puccinia graminis (Pgr Trz1) and S. punctatus (SpuTrz1). Non-fungal tRNase ZLs are from A. thaliana (AthTrz4) [13], D. melanogaster (DmeTrz1) [54] and Homo sapiens (HsaTrz2) [9]. Protein accession numbers are described in Table 1. The alignment was constructed using the program Clustal W [49]. Identical residues are on a black background and conserved residues shaded in gray. Also indicated above the sequence alignment are the conserved motifs involved in substrate binding and catalysis. The conserved motifs are labeled according to references [30, 31, 44]. Numbers in parentheses are the positions of the amino acid sequences. The numbers in brackets indicate the length of the region in tRNase Z, which are species-specific and could not be correctly aligned. Hyphens represent gaps introduced into sequences for maximum alignment. The positions of amino acid residues of the D. melanogaster tRNase ZL critical for catalytic efficiency [30, 31] are indicated by asterisk.