| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KZL35967.1 | KZL39198.1 | TY91_14435 | TY91_10645 | Peptidase M13; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dipeptidase PepV; Divalent metal ion-dependent extracellular dipeptidase; able to hydrolyze a broad range of dipeptides but no tri-, tetra-, or larger oligopeptides; differences in the amino acid specificity of the cleavage site varies between species; similar to succinyl-diaminopimelate desuccinylases; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.547 |
| KZL35967.1 | KZL39337.1 | TY91_14435 | TY91_10005 | Peptidase M13; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.632 |
| KZL35967.1 | KZL41493.1 | TY91_14435 | TY91_07015 | Peptidase M13; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dipeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.692 |
| KZL35967.1 | KZL42780.1 | TY91_14435 | TY91_03735 | Peptidase M13; Derived by automated computational analysis using gene prediction method: Protein Homology. | Oligopeptidase PepB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.549 |
| KZL35967.1 | map-2 | TY91_14435 | TY91_14495 | Peptidase M13; Derived by automated computational analysis using gene prediction method: Protein Homology. | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.457 |
| KZL35967.1 | pepT | TY91_14435 | TY91_07150 | Peptidase M13; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | 0.554 |
| KZL35967.1 | pepX | TY91_14435 | TY91_09165 | Peptidase M13; Derived by automated computational analysis using gene prediction method: Protein Homology. | X-prolyl-dipeptidyl aminopeptidase; Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline; Belongs to the peptidase S15 family. | 0.553 |
| KZL39198.1 | KZL35967.1 | TY91_10645 | TY91_14435 | Dipeptidase PepV; Divalent metal ion-dependent extracellular dipeptidase; able to hydrolyze a broad range of dipeptides but no tri-, tetra-, or larger oligopeptides; differences in the amino acid specificity of the cleavage site varies between species; similar to succinyl-diaminopimelate desuccinylases; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase M13; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.547 |
| KZL39198.1 | KZL39337.1 | TY91_10645 | TY91_10005 | Dipeptidase PepV; Divalent metal ion-dependent extracellular dipeptidase; able to hydrolyze a broad range of dipeptides but no tri-, tetra-, or larger oligopeptides; differences in the amino acid specificity of the cleavage site varies between species; similar to succinyl-diaminopimelate desuccinylases; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.739 |
| KZL39198.1 | KZL41493.1 | TY91_10645 | TY91_07015 | Dipeptidase PepV; Divalent metal ion-dependent extracellular dipeptidase; able to hydrolyze a broad range of dipeptides but no tri-, tetra-, or larger oligopeptides; differences in the amino acid specificity of the cleavage site varies between species; similar to succinyl-diaminopimelate desuccinylases; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dipeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.546 |
| KZL39198.1 | map-2 | TY91_10645 | TY91_14495 | Dipeptidase PepV; Divalent metal ion-dependent extracellular dipeptidase; able to hydrolyze a broad range of dipeptides but no tri-, tetra-, or larger oligopeptides; differences in the amino acid specificity of the cleavage site varies between species; similar to succinyl-diaminopimelate desuccinylases; Derived by automated computational analysis using gene prediction method: Protein Homology. | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.411 |
| KZL39198.1 | pepT | TY91_10645 | TY91_07150 | Dipeptidase PepV; Divalent metal ion-dependent extracellular dipeptidase; able to hydrolyze a broad range of dipeptides but no tri-, tetra-, or larger oligopeptides; differences in the amino acid specificity of the cleavage site varies between species; similar to succinyl-diaminopimelate desuccinylases; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | 0.692 |
| KZL39198.1 | pepX | TY91_10645 | TY91_09165 | Dipeptidase PepV; Divalent metal ion-dependent extracellular dipeptidase; able to hydrolyze a broad range of dipeptides but no tri-, tetra-, or larger oligopeptides; differences in the amino acid specificity of the cleavage site varies between species; similar to succinyl-diaminopimelate desuccinylases; Derived by automated computational analysis using gene prediction method: Protein Homology. | X-prolyl-dipeptidyl aminopeptidase; Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline; Belongs to the peptidase S15 family. | 0.542 |
| KZL39337.1 | KZL35967.1 | TY91_10005 | TY91_14435 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase M13; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.632 |
| KZL39337.1 | KZL39198.1 | TY91_10005 | TY91_10645 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dipeptidase PepV; Divalent metal ion-dependent extracellular dipeptidase; able to hydrolyze a broad range of dipeptides but no tri-, tetra-, or larger oligopeptides; differences in the amino acid specificity of the cleavage site varies between species; similar to succinyl-diaminopimelate desuccinylases; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.739 |
| KZL39337.1 | KZL41493.1 | TY91_10005 | TY91_07015 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dipeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.719 |
| KZL39337.1 | KZL42780.1 | TY91_10005 | TY91_03735 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Oligopeptidase PepB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.548 |
| KZL39337.1 | map-2 | TY91_10005 | TY91_14495 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.619 |
| KZL39337.1 | pepT | TY91_10005 | TY91_07150 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family. | 0.776 |
| KZL39337.1 | pepX | TY91_10005 | TY91_09165 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | X-prolyl-dipeptidyl aminopeptidase; Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline; Belongs to the peptidase S15 family. | 0.784 |