Electronic Journal of Biotechnology ISSN: 0717-3458
  © 2004 by Universidad Católica de Valparaíso -- Chile
Vol. 7 No. 3, Issue of December 15, 2004

Figure 3. Comparisons of deduced amino acid sequence of peanut glycinin peanut Gly-1 (Acc #AF125192, gi|9864776) with sequences from soybean Gy2 (gi|18636) and Gy3 gi|18638) subunit; V. sativa legumin A (gi|483448) and V. faba legumin A2 gi|100101) comparing conserved residues and binding motifs.
Numbering on the left indicates the sequence of corresponding residue.
Gaps have been introduced to maximize alignments.
Dashes indicate gaps introduced to maximize alignment.
Dots indicate identical amino acid residues to peanut Gly-1 clone.
Cysteine residues marked by an astrick (*) involved in interchain linkages, whereas those marked by a cap (^) identify conserved residues possibly involved in interchain linkages.
The signal peptide (SP) are shown by a straight (____) line, cleavage site NG indicated by the vertical arrowhead (residue 344/345 and residue 431/432); Glycosylation signals (NXS) are in bold and underlined.
Regions homologous to variable regions I and II (VR1, VR2) and to the hypervariable region (HVR) known from other glycinin is indicated by broken (----) line.
The consensus cupin signature residues are in highlighted, the metal-binding active site ligands of two histidines and a glutamate are in bold.
Doubly underlined residues indicate conserved a-subunit region of typical glycinin/legumin gene family.

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