Characterization of a Moniezia expansa ubiquitin-conjugating enzyme E2 cDNA.

Ubiquitin and other ubiquitin-like proteins play important roles in post-translational modification. They are phylogenetically well-conserved in eukaryotes. Here we report a new ubiquitin-conjugating enzyme E2 cDNA, which containing a ubiquitin-conjugating enzyme UBCc-domain named UBE2AM. Its cDNA is 899 base pairs in length and contains an open reading frame from nucleotide 171 to 632 encoding 153 amino acids. The result of real time RT-PCR showed that UBEA2 M is expressed in most of M. expansa proglottides and over-expressed in the mature proglottides. Comparison of predicted UBE2AM with UBCc (protein) homologues/orthologous from other species revealed identities between species varying from 97.5 to 99.4% at the amino acid level. Phylogenetic analysis showed the UBE2AM is a member of the eukaryotic UBCc superfamily, which have diverged from a common ancestor and the gene is clustered in the same group with the ubiquitin-conjugating enzyme E2A-like protein from Taenia asiatica.