node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
aqpZ | ybjD | b0875 | b0876 | Aquaporin Z; Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | 0.538 |
aqpZ | ybjE | b0875 | b0874 | Aquaporin Z; Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. | Putative transporter; Mediates export of lysine; Belongs to the LysO family. | 0.770 |
bglH | ybjD | b3720 | b0876 | Carbohydrate-specific outer membrane porin, cryptic; Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin. | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | 0.564 |
csiE | flgA | b2535 | b1072 | Stationary phase inducible protein. | Assembly protein for flagellar basal-body periplasmic P ring; Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P- ring assembly; Belongs to the FlgA family. | 0.741 |
csiE | ybjD | b2535 | b0876 | Stationary phase inducible protein. | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | 0.615 |
flgA | csiE | b1072 | b2535 | Assembly protein for flagellar basal-body periplasmic P ring; Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P- ring assembly; Belongs to the FlgA family. | Stationary phase inducible protein. | 0.741 |
flgA | ybjD | b1072 | b0876 | Assembly protein for flagellar basal-body periplasmic P ring; Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P- ring assembly; Belongs to the FlgA family. | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | 0.566 |
frsA | ybjD | b0239 | b0876 | Fermentation-respiration switch protein; Displays esterase activity toward pNP-butyrate. | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | 0.512 |
hsdM | hsdS | b4349 | b4348 | DNA methyltransferase M; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the [...] | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | 0.999 |
hsdM | ybjD | b4349 | b0876 | DNA methyltransferase M; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the [...] | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | 0.689 |
hsdS | hsdM | b4348 | b4349 | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | DNA methyltransferase M; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the [...] | 0.999 |
hsdS | ybjD | b4348 | b0876 | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | 0.795 |
intE | ybjD | b1140 | b0876 | E14 prophage; Integrase from the cryptic lambdoic prophage e14. Integrase is necessary for integration of the phage into the host genome by site- specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome. | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | 0.478 |
ybjD | aqpZ | b0876 | b0875 | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | Aquaporin Z; Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. | 0.538 |
ybjD | bglH | b0876 | b3720 | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | Carbohydrate-specific outer membrane porin, cryptic; Part of a cryptic operon that is poorly expressed in vivo. May be an ancestral sugar porin with a broad carbohydrate specificity; it binds aromatic beta-D-glucosides such as arbutin and salicin, but with low affinity compared to the binding of maltooligosaccharides to the LamB porin. | 0.564 |
ybjD | csiE | b0876 | b2535 | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | Stationary phase inducible protein. | 0.615 |
ybjD | flgA | b0876 | b1072 | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | Assembly protein for flagellar basal-body periplasmic P ring; Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P- ring assembly; Belongs to the FlgA family. | 0.566 |
ybjD | frsA | b0876 | b0239 | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | Fermentation-respiration switch protein; Displays esterase activity toward pNP-butyrate. | 0.512 |
ybjD | hsdM | b0876 | b4349 | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | DNA methyltransferase M; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the [...] | 0.689 |
ybjD | hsdS | b0876 | b4348 | Putative OLD family ATP-dependent endonuclease; DUF2813 family protein. | Specificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] | 0.795 |