Fig. 1.

Nucleotide (lower case text) and deduced amino acid (upper case text) sequences of hovi-meh1 and Hovi-mEH1, respectively. The 5′- and 3′-UTR sequences, and coding sequence of hovi-meh1 were 174, 101, and 1,374 nts-long, respectively. Amino acid residues that form the putative catalytic triad (D-227, H-432, and E-405), oxyanion hole (Y-300 and Y-375), and HGWP motif (residues 152-155) are shown in bold text. The asterisk indicates a stop codon (TAG). A putative membrane anchor domain (residues 2-24) that was predicted by SOSUI version 1.11 (Hirokawa et al. 1998) is shown in italic text. A predicted cleavage and polyadenylation specificity factor (CPSF) complex binding site is underlined. Amino acid residue positions are indicated to the right.