node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Sbal_2022 | Sbal_2272 | Sbal_2022 | Sbal_2272 | KEGG: shn:Shewana3_1936 thiamine biosynthesis protein ThiC. | PFAM: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | 0.452 |
Sbal_2272 | Sbal_2022 | Sbal_2272 | Sbal_2022 | PFAM: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | KEGG: shn:Shewana3_1936 thiamine biosynthesis protein ThiC. | 0.452 |
Sbal_2272 | Sbal_2273 | Sbal_2272 | Sbal_2273 | PFAM: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | PFAM: Lytic transglycosylase, catalytic; KEGG: shm:Shewmr7_1863 lytic transglycosylase, catalytic. | 0.532 |
Sbal_2272 | Sbal_3176 | Sbal_2272 | Sbal_3176 | PFAM: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | PFAM: protein of unknown function DUF88; KEGG: sdn:Sden_0372 protein of unknown function DUF88. | 0.432 |
Sbal_2272 | lepA | Sbal_2272 | Sbal_1199 | PFAM: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.401 |
Sbal_2272 | map | Sbal_2272 | Sbal_1449 | PFAM: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | 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. | 0.554 |
Sbal_2272 | msrP | Sbal_2272 | Sbal_2271 | PFAM: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | Oxidoreductase, molybdopterin binding; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce [...] | 0.440 |
Sbal_2273 | Sbal_2272 | Sbal_2273 | Sbal_2272 | PFAM: Lytic transglycosylase, catalytic; KEGG: shm:Shewmr7_1863 lytic transglycosylase, catalytic. | PFAM: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | 0.532 |
Sbal_3176 | Sbal_2272 | Sbal_3176 | Sbal_2272 | PFAM: protein of unknown function DUF88; KEGG: sdn:Sden_0372 protein of unknown function DUF88. | PFAM: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | 0.432 |
lepA | Sbal_2272 | Sbal_1199 | Sbal_2272 | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | PFAM: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | 0.401 |
lepA | map | Sbal_1199 | Sbal_1449 | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 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. | 0.701 |
map | Sbal_2272 | Sbal_1449 | Sbal_2272 | 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: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | 0.554 |
map | lepA | Sbal_1449 | Sbal_1199 | 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. | GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.701 |
msrP | Sbal_2272 | Sbal_2271 | Sbal_2272 | Oxidoreductase, molybdopterin binding; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce [...] | PFAM: protein of unknown function DUF195; KEGG: son:SO2041 hypothetical protein. | 0.440 |