Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair.

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 of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair.

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.

Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair.

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 [...]

Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair.

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 XerD 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 [...]

Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair.

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 [...]

DNA cytosine methyltransferase; This methylase recognizes the double-stranded sequence CCWGG, causes specific methylation on C-2 on both strands.

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 cytosine methyltransferase; This methylase recognizes the double-stranded sequence CCWGG, causes specific methylation on C-2 on both strands.

DNA mismatch endonuclease of very short patch repair; Deamination of 5-methylcytosine in DNA results in T/G mismatches. If unrepaired, these mismatches can lead to C-to-C transition mutations. The very short patch (VSP) repair process in E.coli counteracts the mutagenic process by repairing the mismatches in favor of the G-containing strand. This enzyme is an endonuclease that nicks double-stranded DNA within the sequence CT(AT)GN or NT(AT)GG next to the thymidine residue that is mismatched to 2'-deoxyguanosine. The incision is mismatch-dependent and strand-specific; Belongs to the vsr [...]

DNA cytosine methyltransferase; This methylase recognizes the double-stranded sequence CCWGG, causes specific methylation on C-2 on both strands.

Putative HD superfamily phosphohydrolase.

DNA cytosine methyltransferase; This methylase recognizes the double-stranded sequence CCWGG, causes specific methylation on C-2 on both strands.

Inner membrane 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 [...]

Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair.

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 cytosine methyltransferase; This methylase recognizes the double-stranded sequence CCWGG, causes specific methylation on C-2 on both strands.

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.

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 [...]

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 5-methylcytosine/5-hydroxymethylcytosine-specific restriction nuclease; Restriction of 5-methyl and 5-hydroxymethylcytosines at the specific DNA sequence C(me)CGG.

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.

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 [...]

Protein McrC; Modifies the specificity of McrB restriction by expanding the range of modified sequences restricted. Does not bind to DNA.

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.

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 XerD 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 [...]

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 [...]

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.

Endonuclease of nucleotide excision repair; Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair.