ThiD-TenA: a gene pair fusion in eukaryotes.
Computational analysis of the hypothetical open reading frame MJ0236 from Methanococcus jannaschii reveals its membership to a family of bacterial and eukaryotic proteins, predicted to be the HMP-P kinases involved in thiamin biosyntheis (ThiD). The eukaryotic members of this family contain a C-terminal extension similar to a bacterial transcriptional activator (TenA), thus pointing to a fusion event that took place during cellular evolution. The C-terminal domain is absent from M. jannaschii. The significance of this observation is two-fold: first, this is a case where a fusion protein contains two domains with an unusual phylogenetic distribution, and second, the TenA domain is a rare case of a gene family involved in transcription present both in bacteria and eukaryotes.
Ouzounis
C A
CA
Kyrpides
N C
NC
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics; D004268:DNA-Binding Proteins / Q000235:genetics*; D019143:Evolution, Molecular; D005656:Fungal Proteins / Q000235:genetics; D017017:Methanococcus / Q000235:genetics*; D008969:Molecular Sequence Data; D005810:Multigene Family; D017856:Phosphotransferases (Phosphate Group Acceptor) / Q000235:genetics*; D011995:Recombination, Genetic; D017386:Sequence Homology, Amino Acid; D013831:Thiamine / Q000235:genetics; D014157:Transcription Factors / Q000235:genetics*
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D014157:Transcription Factors; C108436:4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate kinase; D017856:Phosphotransferases (Phosphate Group Acceptor); D013831:Thiamine