We reported previously that the carboxy-terminal 30 amino acids of SUPERMAN (SUPRD) function as a repression domain in Arabidopsis. In this study, we identified the peptide sequences in SUPRD that is both necessary and sufficient for repression of transcription. To our surprise, the hexapeptide DLELRL was sufficient, by itself, to confer the ability to repress transcription on a DNA-binding domain. A database search revealed that there are 32 TFIIIA-type zinc finger proteins in the Arabidopsis genome that contain a hexapeptide sequence similar or identical to that of DLELRL. These peptides acted as repression domains, suggesting that these zinc finger proteins might function as active repressors. Further mutational analysis within DLELRL revealed that an amphiphilic motif composed of six amino acids (XLxLXL) with preferences at the first and fifth positions is necessary and sufficient for strong repression. An assay of positional effects suggested that GAL4DB-DLELRL might function as a short-range repressor. A possible mechanism of the DLELRL-mediated repression is discussed.