Amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the archaebacterium Halobacterium marismortui.
The complete amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the archaebacterium Halobacterium marismortui were determined. Protein HL30 was found to be acetylated at its N-terminal amino acid and shows homology to the eukaryotic ribosomal proteins YL34 from yeast and RL31 from rat. Protein HmaL5 was homologous to the protein L5 from Escherichia coli and Bacillus stearothermophilus as well as to YL16 from yeast. HmaL5 shows more similarities to its eukaryotic counterpart than to eubacterial ones.
Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin, Germany.
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D000595:Amino Acid Sequence; D000818:Animals; D019843:Archaeal Proteins; D004926:Escherichia coli / Q000235:genetics; D001411:Geobacillus stearothermophilus / Q000235:genetics; D006217:Halobacterium / Q000235:genetics*; D008969:Molecular Sequence Data; D051381:Rats; D012269:Ribosomal Proteins / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
D019843:Archaeal Proteins; C065230:HL30 protein, Halobacterium marismortui; D012269:Ribosomal Proteins; C065232:ribosomal protein HmaL5, Haloarcula marismortui