Fig. 2.
Fig. 2. Comparison of the predicted amino acid sequences withMDS1/EVI1 and MEL1. / (A) Alignment of the predicted amino acid sequences of the humanMEL1 (upper) and MDS1/EVI1 (lower) proteins. ‘*’ indicates identical amino acids, ‘:’ and ‘.’ indicate similar amino acids, and ‘–’ represents a gap that has been introduced to optimize the homology. The sequences were compared by the Clustalw program of The EMBL-European Bioinformatics Institute (EBI). Underlines indicate the position of metal binding cysteines and histidines in zinc finger motif. (B) Comparison of the domain structure betweenMDS1/EVI1 and MEL1. Each abbreviation is indicated by the following letters: PRD, PR domain; DBD-1, DNA binding domain-1; PRR, proline-rich domain; RD, repressor domain; DB-2, DNA binding domain-2; AD, acidic domain. (C) Sequence comparison of the conserved PR domain among RIZ, BLIMP1, MDS1/EVI1, and MEL1.

Comparison of the predicted amino acid sequences withMDS1/EVI1 and MEL1.

(A) Alignment of the predicted amino acid sequences of the humanMEL1 (upper) and MDS1/EVI1 (lower) proteins. ‘*’ indicates identical amino acids, ‘:’ and ‘.’ indicate similar amino acids, and ‘–’ represents a gap that has been introduced to optimize the homology. The sequences were compared by the Clustalw program of The EMBL-European Bioinformatics Institute (EBI). Underlines indicate the position of metal binding cysteines and histidines in zinc finger motif. (B) Comparison of the domain structure betweenMDS1/EVI1 and MEL1. Each abbreviation is indicated by the following letters: PRD, PR domain; DBD-1, DNA binding domain-1; PRR, proline-rich domain; RD, repressor domain; DB-2, DNA binding domain-2; AD, acidic domain. (C) Sequence comparison of the conserved PR domain among RIZ, BLIMP1, MDS1/EVI1, and MEL1.

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