Identification of protein-tyrosine phosphatases in Archaea.
Protein-tyrosine dephosphorylation is a major mechanism in cellular regulation. A large number of protein-tyrosine phosphatases is known from Eukarya, and more recently bacterial homologues have also been identified. By employing conserved sequence patterns from both eukaryotic and bacterial protein-tyrosine phosphatases, we have identified three homologous sequences in two of the four complete archaeal genomes. Two hypothetical open reading frames in the genome of Methanococcus jannaschii (MJ0215 and MJECL20) and one in the genome of Pyrococcus horikoshii (PH1732) clearly bear all the conserved residues of this family. No homologues were found in the genomes of Archaeoglobus fulgidus and Methanobacterium thermoautotrophicum. This is the first report of protein-tyrosine phosphatase sequences in Archaea.
Stravopodis
D J
DJ
Kyrpides
N C
NC
D000595:Amino Acid Sequence; D001105:Archaea / Q000201:enzymology* / Q000235:genetics*; D019611:Archaeoglobus fulgidus / Q000201:enzymology / Q000235:genetics; D017124:Conserved Sequence; D019143:Evolution, Molecular; D016678:Genome; D017014:Methanobacterium / Q000201:enzymology / Q000235:genetics; D017017:Methanococcus / Q000201:enzymology / Q000235:genetics; D008969:Molecular Sequence Data; D017027:Protein Tyrosine Phosphatases / Q000235:genetics*; D019711:Pyrococcus / Q000201:enzymology / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D017027:Protein Tyrosine Phosphatases