| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Slit_0383 | Slit_1664 | Slit_0383 | Slit_1664 | PFAM: protein of unknown function DUF497; KEGG: pph:Ppha_2521 hypothetical protein. | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | 0.456 |
| Slit_1434 | Slit_1664 | Slit_1434 | Slit_1664 | PFAM: MltA-interacting MipA family protein; KEGG: pnu:Pnuc_2040 MltA-interacting MipA family protein. | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | 0.677 |
| Slit_1664 | Slit_0383 | Slit_1664 | Slit_0383 | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | PFAM: protein of unknown function DUF497; KEGG: pph:Ppha_2521 hypothetical protein. | 0.456 |
| Slit_1664 | Slit_1434 | Slit_1664 | Slit_1434 | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | PFAM: MltA-interacting MipA family protein; KEGG: pnu:Pnuc_2040 MltA-interacting MipA family protein. | 0.677 |
| Slit_1664 | Slit_1665 | Slit_1664 | Slit_1665 | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | PFAM: extracellular solute-binding protein family 1; KEGG: rfr:Rfer_3242 extracellular solute-binding protein. | 0.597 |
| Slit_1664 | Slit_1666 | Slit_1664 | Slit_1666 | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | Diguanylate cyclase/phosphodiesterase with PAS/PAC and GAF sensor(s); SMART: EAL domain protein; GGDEF domain containing protein; PAS domain containing protein; PAC repeat-containing protein; histidine kinase HAMP region domain protein; GAF domain protein; TIGRFAM: diguanylate cyclase; PAS sensor protein; KEGG: mfa:Mfla_2628 diguanylate cyclase/phosphodiesterase; PFAM: EAL domain protein; PAS fold-4 domain protein; histidine kinase HAMP region domain protein; GGDEF domain containing protein; GAF domain protein. | 0.438 |
| Slit_1664 | glnD | Slit_1664 | Slit_1663 | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | UTP-GlnB uridylyltransferase, GlnD; 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 assimilation and metabolism. | 0.432 |
| Slit_1664 | map | Slit_1664 | Slit_1662 | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | 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. | 0.415 |
| Slit_1665 | Slit_1664 | Slit_1665 | Slit_1664 | PFAM: extracellular solute-binding protein family 1; KEGG: rfr:Rfer_3242 extracellular solute-binding protein. | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | 0.597 |
| Slit_1665 | Slit_1666 | Slit_1665 | Slit_1666 | PFAM: extracellular solute-binding protein family 1; KEGG: rfr:Rfer_3242 extracellular solute-binding protein. | Diguanylate cyclase/phosphodiesterase with PAS/PAC and GAF sensor(s); SMART: EAL domain protein; GGDEF domain containing protein; PAS domain containing protein; PAC repeat-containing protein; histidine kinase HAMP region domain protein; GAF domain protein; TIGRFAM: diguanylate cyclase; PAS sensor protein; KEGG: mfa:Mfla_2628 diguanylate cyclase/phosphodiesterase; PFAM: EAL domain protein; PAS fold-4 domain protein; histidine kinase HAMP region domain protein; GGDEF domain containing protein; GAF domain protein. | 0.663 |
| Slit_1666 | Slit_1664 | Slit_1666 | Slit_1664 | Diguanylate cyclase/phosphodiesterase with PAS/PAC and GAF sensor(s); SMART: EAL domain protein; GGDEF domain containing protein; PAS domain containing protein; PAC repeat-containing protein; histidine kinase HAMP region domain protein; GAF domain protein; TIGRFAM: diguanylate cyclase; PAS sensor protein; KEGG: mfa:Mfla_2628 diguanylate cyclase/phosphodiesterase; PFAM: EAL domain protein; PAS fold-4 domain protein; histidine kinase HAMP region domain protein; GGDEF domain containing protein; GAF domain protein. | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | 0.438 |
| Slit_1666 | Slit_1665 | Slit_1666 | Slit_1665 | Diguanylate cyclase/phosphodiesterase with PAS/PAC and GAF sensor(s); SMART: EAL domain protein; GGDEF domain containing protein; PAS domain containing protein; PAC repeat-containing protein; histidine kinase HAMP region domain protein; GAF domain protein; TIGRFAM: diguanylate cyclase; PAS sensor protein; KEGG: mfa:Mfla_2628 diguanylate cyclase/phosphodiesterase; PFAM: EAL domain protein; PAS fold-4 domain protein; histidine kinase HAMP region domain protein; GGDEF domain containing protein; GAF domain protein. | PFAM: extracellular solute-binding protein family 1; KEGG: rfr:Rfer_3242 extracellular solute-binding protein. | 0.663 |
| glnD | Slit_1664 | Slit_1663 | Slit_1664 | UTP-GlnB uridylyltransferase, GlnD; 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 assimilation and metabolism. | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | 0.432 |
| glnD | map | Slit_1663 | Slit_1662 | UTP-GlnB uridylyltransferase, GlnD; 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 assimilation and 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. | 0.803 |
| map | Slit_1664 | Slit_1662 | Slit_1664 | 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. | PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor. | 0.415 |
| map | glnD | Slit_1662 | Slit_1663 | 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. | UTP-GlnB uridylyltransferase, GlnD; 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 assimilation and metabolism. | 0.803 |