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Conserved amino acid residues within the MAGE protein family.

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posted on 25.02.2011 by Jessica J. R. Hudson, Katerina Bednarova, Lucie Kozakova, Chunyan Liao, Marc Guerineau, Rita Colnaghi, Susanne Vidot, Jaromir Marek, Sreenivas R. Bathula, Alan R. Lehmann, Jan Palecek

Alignment of the N-terminal (A) (aa 89 to 199 of S.p. Nse3) and C-terminal (B) (aa 211 to 301 of S.p. Nse3) part of MHD domain of Nse3/MAGEG1 subfamily. The Nse3/MAGEG1 orthologs are from S. pombe (S.p.), Aspergillus nidulans (A.n.), Neosartorya fischeri (N.f.), Aspergillus terreus (A.t.), Aspergillus clavatus (A.c.), Neurospora crassa (N.c.), Magnaporthe grisea (M.g.), Aspergillus oryzae (A.o.), S. cerevisiae (S.c.), Danio rerio (D.r.), Xenopus tropicalis (X.t.), Galus galus (G.g.), Ornithorhynchus anatinus (O.a.), Monodelphis domestica (M.d.), Dasypus novemcinctus (D.n.), Canis lupus familiaris (C.f.), Mus musculus (M.m.), Homo sapiens (H.s.). Secondary structure derived from the 3D-structure model of Nse3 is indicated above the alignment: cyan rectangle, helix; orange arrow, beta-sheet. Most of the conserved residues were mutated (mut) in the S. pombe Nse3 sequence to alanine; m, mutated residue; red rectangles indicate Nse1- and/or Nse4-specific mutants, respectively; Y264 and L265 residues are labelled with asterisk (B). NSE4b-specific residues of MAGEG1 protein are also indicated in red below the MAGEG1 sequence (B). (C) Alignment of C-terminal part of MHD domain of human MAGE proteins. Shading represents amino acid groups conserved across the family: dark green, hydrophobic and aromatic; light green, polar; blue, acidic; pink, basic; all glycine and proline residues are highlighted in yellow.