node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MGYG_00254 | MGYG_00710 | E5QYC0 | E5R1B9 | Serpin B6; Belongs to the serpin family. | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | 0.598 |
MGYG_00254 | MGYG_04088 | E5QYC0 | E4UUW8 | Serpin B6; Belongs to the serpin family. | ANK_REP_REGION domain-containing protein. | 0.550 |
MGYG_00254 | MGYG_05176 | E5QYC0 | E4UYL0 | Serpin B6; Belongs to the serpin family. | Uncharacterized protein. | 0.809 |
MGYG_00710 | MGYG_00254 | E5R1B9 | E5QYC0 | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | Serpin B6; Belongs to the serpin family. | 0.598 |
MGYG_00710 | MGYG_00974 | E5R1B9 | E5R3C2 | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | pH-response transcription factor pacC/RIM101. | 0.433 |
MGYG_00710 | MGYG_03059 | E5R1B9 | E4UQN5 | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | pH-response regulator protein palF/RIM8. | 0.524 |
MGYG_00710 | MGYG_03481 | E5R1B9 | E4US61 | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | Reticulon-like protein. | 0.562 |
MGYG_00710 | MGYG_04060 | E5R1B9 | E4UUU0 | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | A-factor-processing enzyme. | 0.545 |
MGYG_00710 | MGYG_04088 | E5R1B9 | E4UUW8 | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | ANK_REP_REGION domain-containing protein. | 0.528 |
MGYG_00710 | MGYG_05176 | E5R1B9 | E4UYL0 | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | Uncharacterized protein. | 0.713 |
MGYG_00710 | MGYG_05821 | E5R1B9 | E4UY41 | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | pH-response regulator protein palI/RIM9. | 0.523 |
MGYG_00710 | MGYG_07179 | E5R1B9 | E4V2A7 | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | Importin subunit beta-1. | 0.429 |
MGYG_00710 | MGYG_09204 | E5R1B9 | E4V6T8 | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | P/Homo B domain-containing protein. | 0.427 |
MGYG_00974 | MGYG_00710 | E5R3C2 | E5R1B9 | pH-response transcription factor pacC/RIM101. | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | 0.433 |
MGYG_00974 | MGYG_03059 | E5R3C2 | E4UQN5 | pH-response transcription factor pacC/RIM101. | pH-response regulator protein palF/RIM8. | 0.777 |
MGYG_00974 | MGYG_04088 | E5R3C2 | E4UUW8 | pH-response transcription factor pacC/RIM101. | ANK_REP_REGION domain-containing protein. | 0.581 |
MGYG_00974 | MGYG_05821 | E5R3C2 | E4UY41 | pH-response transcription factor pacC/RIM101. | pH-response regulator protein palI/RIM9. | 0.702 |
MGYG_03059 | MGYG_00710 | E4UQN5 | E5R1B9 | pH-response regulator protein palF/RIM8. | Aspartic protease pepA; Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | 0.524 |
MGYG_03059 | MGYG_00974 | E4UQN5 | E5R3C2 | pH-response regulator protein palF/RIM8. | pH-response transcription factor pacC/RIM101. | 0.777 |
MGYG_03059 | MGYG_05821 | E4UQN5 | E4UY41 | pH-response regulator protein palF/RIM8. | pH-response regulator protein palI/RIM9. | 0.609 |