node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EAR61495.1 | EAR63038.1 | MED92_18353 | MED92_07961 | Molybdenum cofactor biosynthesis protein B; COG0521 Molybdopterin biosynthesis enzymes. | COG3492 Uncharacterized protein conserved in bacteria. | 0.706 |
EAR62249.1 | EAR63038.1 | MED92_14468 | MED92_07961 | Hypothetical protein; COG0621 2-methylthioadenine synthetase. | COG3492 Uncharacterized protein conserved in bacteria. | 0.682 |
EAR63038.1 | EAR61495.1 | MED92_07961 | MED92_18353 | COG3492 Uncharacterized protein conserved in bacteria. | Molybdenum cofactor biosynthesis protein B; COG0521 Molybdopterin biosynthesis enzymes. | 0.706 |
EAR63038.1 | EAR62249.1 | MED92_07961 | MED92_14468 | COG3492 Uncharacterized protein conserved in bacteria. | Hypothetical protein; COG0621 2-methylthioadenine synthetase. | 0.682 |
EAR63038.1 | glnD | MED92_07961 | MED92_07966 | COG3492 Uncharacterized protein conserved in bacteria. | PII uridylyl-transferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | 0.741 |
EAR63038.1 | map | MED92_07961 | MED92_07971 | COG3492 Uncharacterized protein conserved in bacteria. | Methionine aminopeptidase, type I; 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. | 0.704 |
EAR63038.1 | rpsB | MED92_07961 | MED92_07976 | COG3492 Uncharacterized protein conserved in bacteria. | COG0052 Ribosomal protein S2; Belongs to the universal ribosomal protein uS2 family. | 0.409 |
glnD | EAR63038.1 | MED92_07966 | MED92_07961 | PII uridylyl-transferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | COG3492 Uncharacterized protein conserved in bacteria. | 0.741 |
glnD | map | MED92_07966 | MED92_07971 | PII uridylyl-transferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | Methionine aminopeptidase, type I; 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. | 0.806 |
glnD | rpsB | MED92_07966 | MED92_07976 | PII uridylyl-transferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | COG0052 Ribosomal protein S2; Belongs to the universal ribosomal protein uS2 family. | 0.547 |
map | EAR63038.1 | MED92_07971 | MED92_07961 | Methionine aminopeptidase, type I; 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. | COG3492 Uncharacterized protein conserved in bacteria. | 0.704 |
map | glnD | MED92_07971 | MED92_07966 | Methionine aminopeptidase, type I; 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. | PII uridylyl-transferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | 0.806 |
map | rpsB | MED92_07971 | MED92_07976 | Methionine aminopeptidase, type I; 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. | COG0052 Ribosomal protein S2; Belongs to the universal ribosomal protein uS2 family. | 0.995 |
rpsB | EAR63038.1 | MED92_07976 | MED92_07961 | COG0052 Ribosomal protein S2; Belongs to the universal ribosomal protein uS2 family. | COG3492 Uncharacterized protein conserved in bacteria. | 0.409 |
rpsB | glnD | MED92_07976 | MED92_07966 | COG0052 Ribosomal protein S2; Belongs to the universal ribosomal protein uS2 family. | PII uridylyl-transferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. | 0.547 |
rpsB | map | MED92_07976 | MED92_07971 | COG0052 Ribosomal protein S2; Belongs to the universal ribosomal protein uS2 family. | Methionine aminopeptidase, type I; 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. | 0.995 |