node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
hsdM | hsdR | b4349 | b4350 | 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 [...] | Endonuclease R Type I restriction enzyme; The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification; Belongs to the HsdR family. | 0.999 |
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 | mcrB | b4349 | b4346 | 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 [...] | 5-methylcytosine-specific restriction enzyme McrBC, subunit McrB; Recognizes N4- and C5-methylcytosine (and 5-hydroxy- methylcytosines) produced by a broad range of DNA methylases and appears to act against 5-methylcytosine preceded by a purine residue. Binds to DNA containing methylated cytosines; also binds to GTP. Isoform 33 kDa is less active than isoform 51 kDa and may play a role in regulating the activity of isoform 51 kDa by competing with it in DNA and protein binding abilities. | 0.861 |
hsdM | mrr | b4349 | b4351 | 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 [...] | Methylated adenine and cytosine restriction protein; Involved in the acceptance of foreign DNA which is modified. Restricts both adenine- and cytosine-methylated DNA. | 0.918 |
hsdM | rpsL | b4349 | b3342 | 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 [...] | 30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy. Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit; Belongs to the universal ribosomal protein uS12 family. | 0.611 |
hsdM | ruvC | b4349 | b1863 | 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 [...] | Component of RuvABC resolvasome, endonuclease; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | 0.604 |
hsdM | uvrB | b4349 | b0779 | 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 [...] | Exision nuclease of nucleotide excision repair, DNA damage recognition component; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesi [...] | 0.899 |
hsdM | xerD | b4349 | b2894 | 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 [...] | Site-specific tyrosine recombinase; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerC binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids at ColE1 xer (or cer) and pSC101 (or [...] | 0.633 |
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 |
hsdM | yhdJ | b4349 | b3262 | 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 [...] | DNA adenine methyltransferase, SAM-dependent; Methylates the second adenine of the NsiI recognition sequence (5'-ATGCAT-3'). | 0.798 |
hsdR | hsdM | b4350 | b4349 | Endonuclease R Type I restriction enzyme; The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification; Belongs to the HsdR family. | 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 |
hsdR | hsdS | b4350 | b4348 | Endonuclease R Type I restriction enzyme; The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification; Belongs to the HsdR family. | 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 |
hsdR | mcrB | b4350 | b4346 | Endonuclease R Type I restriction enzyme; The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification; Belongs to the HsdR family. | 5-methylcytosine-specific restriction enzyme McrBC, subunit McrB; Recognizes N4- and C5-methylcytosine (and 5-hydroxy- methylcytosines) produced by a broad range of DNA methylases and appears to act against 5-methylcytosine preceded by a purine residue. Binds to DNA containing methylated cytosines; also binds to GTP. Isoform 33 kDa is less active than isoform 51 kDa and may play a role in regulating the activity of isoform 51 kDa by competing with it in DNA and protein binding abilities. | 0.934 |
hsdR | mrr | b4350 | b4351 | Endonuclease R Type I restriction enzyme; The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification; Belongs to the HsdR family. | Methylated adenine and cytosine restriction protein; Involved in the acceptance of foreign DNA which is modified. Restricts both adenine- and cytosine-methylated DNA. | 0.965 |
hsdR | rpsL | b4350 | b3342 | Endonuclease R Type I restriction enzyme; The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification; Belongs to the HsdR family. | 30S ribosomal subunit protein S12; With S4 and S5 plays an important role in translational accuracy. Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit; Belongs to the universal ribosomal protein uS12 family. | 0.970 |
hsdR | ruvC | b4350 | b1863 | Endonuclease R Type I restriction enzyme; The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification; Belongs to the HsdR family. | Component of RuvABC resolvasome, endonuclease; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | 0.567 |
hsdR | uvrB | b4350 | b0779 | Endonuclease R Type I restriction enzyme; The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification; Belongs to the HsdR family. | Exision nuclease of nucleotide excision repair, DNA damage recognition component; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesi [...] | 0.571 |
hsdR | xerD | b4350 | b2894 | Endonuclease R Type I restriction enzyme; The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification; Belongs to the HsdR family. | Site-specific tyrosine recombinase; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerC binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids at ColE1 xer (or cer) and pSC101 (or [...] | 0.621 |
hsdR | yhdJ | b4350 | b3262 | Endonuclease R Type I restriction enzyme; The EcoKI enzyme recognizes 5'-AACN(6)GTGC-3'. Subunit R is required for both nuclease and ATPase activities, but not for modification; Belongs to the HsdR family. | DNA adenine methyltransferase, SAM-dependent; Methylates the second adenine of the NsiI recognition sequence (5'-ATGCAT-3'). | 0.476 |
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 |