Activating Compound | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | required | Geobacillus stearothermophilus | |
S-adenosyl-L-methionine | required | Lysinibacillus sphaericus | |
S-adenosyl-L-methionine | required | Weizmannia coagulans | |
S-adenosyl-L-methionine | required | Bacillus pumilus | |
S-adenosyl-L-methionine | required | Citrobacter sp. | |
S-adenosyl-L-methionine | required | Acinetobacter lwoffii | |
S-adenosyl-L-methionine | required | Campylobacter jejuni |
Application | Comment | Organism |
---|---|---|
analysis | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Geobacillus stearothermophilus |
analysis | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Lysinibacillus sphaericus |
analysis | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Pseudomonas putida |
analysis | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Neisseria meningitidis |
analysis | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Weizmannia coagulans |
analysis | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Bacillus pumilus |
analysis | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Citrobacter sp. |
analysis | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Haemophilus aegyptius |
analysis | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Acinetobacter lwoffii |
analysis | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Campylobacter jejuni |
molecular biology | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Geobacillus stearothermophilus |
molecular biology | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Lysinibacillus sphaericus |
molecular biology | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Pseudomonas putida |
molecular biology | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Neisseria meningitidis |
molecular biology | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Weizmannia coagulans |
molecular biology | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Bacillus pumilus |
molecular biology | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Citrobacter sp. |
molecular biology | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Haemophilus aegyptius |
molecular biology | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Acinetobacter lwoffii |
molecular biology | type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA | Campylobacter jejuni |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Weizmannia coagulans | the enzyme has the recognition sequence (10/12) CGAN6TGC (12/10), of which it needs 2 on the substrate to be active. It excises 32 bp, and requires S-adenosyl-L-methionine | ? | - |
? | |
additional information | Acinetobacter lwoffii | the enzyme has the recognition sequence (10/12) GCAN6TGC (12/10), of which it needs 2 on the substrate to be active. It excises 32 bp, and requires S-adenosyl-L-methionine | ? | - |
? | |
additional information | Lysinibacillus sphaericus | the enzyme has the recognition sequence (10/15) ACN4GTAYC (12/7), of which it needs 2 on the substrate to be active. It excises 28 bp, and requires S-adenosyl-L-methionine | ? | - |
? | |
additional information | Citrobacter sp. | the enzyme has the recognition sequence (11/13) CAAN5GTGG (12/10), of which it needs 2 on the substrate to be active. It excises 33 bp, and requires S-adenosyl-L-methionine | ? | - |
? | |
additional information | Neisseria meningitidis | the enzyme has the recognition sequence (12/7) RCCGGY (7/12), of which it needs 2 on the substrate to be active. It excises 20 bp, and does not require S-adenosyl-L-methionine | ? | - |
? | |
additional information | Pseudomonas putida | the enzyme has the recognition sequence (7/12) GAACN6CTC (13/8), of which it needs 2 on the substrate to be active. It excises 28 bp, and does not require S-adenosyl-L-methionine | ? | - |
? | |
additional information | Acinetobacter lwoffii | the enzyme has the recognition sequence (7/12) GAACN6TCC (12/7), of which it needs 2 on the substrate to be active. It excises 27 bp, and does not require S-adenosyl-L-methionine | ? | - |
? | |
additional information | Haemophilus aegyptius | the enzyme has the recognition sequence (7/13) GAYN5RTC (14/9). It excises 27 bp, and does not require S-adenosyl-L-methionine | ? | - |
? | |
additional information | Bacillus pumilus | the enzyme has the recognition sequence (8/13) GAGN5CTC (13/8), of which it needs 1 on the substrate to be active. It excises 27 bp, and requires S-adenosyl-L-methionine | ? | - |
? | |
additional information | Campylobacter jejuni | the enzyme has the recognition sequence (8/14) CCAN6GT (15/9): It excises 28 bp, and requires S-adenosyl-L-methionine | ? | - |
? | |
additional information | Geobacillus stearothermophilus | the enzyme has the recognition sequence (9/12) ACN5CTCC (10/7), of which it needs 2 on the substrate to be active. It excises 27 bp, and requires S-adenosyl-L-methionine | ? | - |
? | |
additional information | Citrobacter sp. 2144 | the enzyme has the recognition sequence (11/13) CAAN5GTGG (12/10), of which it needs 2 on the substrate to be active. It excises 33 bp, and requires S-adenosyl-L-methionine | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter lwoffii | - |
- |
- |
Bacillus pumilus | - |
- |
- |
Campylobacter jejuni | - |
- |
- |
Citrobacter sp. | - |
- |
- |
Citrobacter sp. 2144 | - |
- |
- |
Geobacillus stearothermophilus | - |
- |
- |
Haemophilus aegyptius | - |
- |
- |
Lysinibacillus sphaericus | - |
- |
- |
Neisseria meningitidis | - |
- |
- |
Pseudomonas putida | - |
- |
- |
Weizmannia coagulans | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme has the recognition sequence (10/12) CGAN6TGC (12/10), of which it needs 2 on the substrate to be active. It excises 32 bp, and requires S-adenosyl-L-methionine | Weizmannia coagulans | ? | - |
? | |
additional information | the enzyme has the recognition sequence (10/12) GCAN6TGC (12/10), of which it needs 2 on the substrate to be active. It excises 32 bp, and requires S-adenosyl-L-methionine | Acinetobacter lwoffii | ? | - |
? | |
additional information | the enzyme has the recognition sequence (10/15) ACN4GTAYC (12/7), of which it needs 2 on the substrate to be active. It excises 28 bp, and requires S-adenosyl-L-methionine | Lysinibacillus sphaericus | ? | - |
? | |
additional information | the enzyme has the recognition sequence (11/13) CAAN5GTGG (12/10), of which it needs 2 on the substrate to be active. It excises 33 bp, and requires S-adenosyl-L-methionine | Citrobacter sp. | ? | - |
? | |
additional information | the enzyme has the recognition sequence (12/7) RCCGGY (7/12), of which it needs 2 on the substrate to be active. It excises 20 bp, and does not require S-adenosyl-L-methionine | Neisseria meningitidis | ? | - |
? | |
additional information | the enzyme has the recognition sequence (7/12) GAACN6CTC (13/8), of which it needs 2 on the substrate to be active. It excises 28 bp, and does not require S-adenosyl-L-methionine | Pseudomonas putida | ? | - |
? | |
additional information | the enzyme has the recognition sequence (7/12) GAACN6TCC (12/7), of which it needs 2 on the substrate to be active. It excises 27 bp, and does not require S-adenosyl-L-methionine | Acinetobacter lwoffii | ? | - |
? | |
additional information | the enzyme has the recognition sequence (7/13) GAYN5RTC (14/9). It excises 27 bp, and does not require S-adenosyl-L-methionine | Haemophilus aegyptius | ? | - |
? | |
additional information | the enzyme has the recognition sequence (8/13) GAGN5CTC (13/8), of which it needs 1 on the substrate to be active. It excises 27 bp, and requires S-adenosyl-L-methionine | Bacillus pumilus | ? | - |
? | |
additional information | the enzyme has the recognition sequence (8/14) CCAN6GT (15/9): It excises 28 bp, and requires S-adenosyl-L-methionine | Campylobacter jejuni | ? | - |
? | |
additional information | the enzyme has the recognition sequence (9/12) ACN5CTCC (10/7), of which it needs 2 on the substrate to be active. It excises 27 bp, and requires S-adenosyl-L-methionine | Geobacillus stearothermophilus | ? | - |
? | |
additional information | the enzyme has the recognition sequence (11/13) CAAN5GTGG (12/10), of which it needs 2 on the substrate to be active. It excises 33 bp, and requires S-adenosyl-L-methionine | Citrobacter sp. 2144 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Lysinibacillus sphaericus |
heterodimer | - |
Weizmannia coagulans |
heterodimer | - |
Bacillus pumilus |
monomer | - |
Pseudomonas putida |
monomer | - |
Haemophilus aegyptius |
monomer | - |
Acinetobacter lwoffii |
monomer | - |
Campylobacter jejuni |
More | consists of two different polypeptide chains R and M | Neisseria meningitidis |
Synonyms | Comment | Organism |
---|---|---|
AlfI | - |
Acinetobacter lwoffii |
AloI | - |
Acinetobacter lwoffii |
BaeI | - |
Lysinibacillus sphaericus |
BcgI | - |
Weizmannia coagulans |
BplI | - |
Bacillus pumilus |
BsaXI | - |
Geobacillus stearothermophilus |
CjeI | - |
Campylobacter jejuni |
CspCI | - |
Citrobacter sp. |
HaeVI | - |
Haemophilus aegyptius |
NmeDI | - |
Neisseria meningitidis |
PPII | - |
Pseudomonas putida |
type II REase | - |
Geobacillus stearothermophilus |
type II REase | - |
Lysinibacillus sphaericus |
type II REase | - |
Pseudomonas putida |
type II REase | - |
Neisseria meningitidis |
type II REase | - |
Weizmannia coagulans |
type II REase | - |
Bacillus pumilus |
type II REase | - |
Citrobacter sp. |
type II REase | - |
Haemophilus aegyptius |
type II REase | - |
Acinetobacter lwoffii |
type II REase | - |
Campylobacter jejuni |
type IIB restriction endonuclease | - |
Geobacillus stearothermophilus |
type IIB restriction endonuclease | - |
Lysinibacillus sphaericus |
type IIB restriction endonuclease | - |
Pseudomonas putida |
type IIB restriction endonuclease | - |
Neisseria meningitidis |
type IIB restriction endonuclease | - |
Weizmannia coagulans |
type IIB restriction endonuclease | - |
Bacillus pumilus |
type IIB restriction endonuclease | - |
Citrobacter sp. |
type IIB restriction endonuclease | - |
Haemophilus aegyptius |
type IIB restriction endonuclease | - |
Acinetobacter lwoffii |
type IIB restriction endonuclease | - |
Campylobacter jejuni |
General Information | Comment | Organism |
---|---|---|
evolution | the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems | Geobacillus stearothermophilus |
evolution | the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems | Lysinibacillus sphaericus |
evolution | the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems | Pseudomonas putida |
evolution | the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems | Neisseria meningitidis |
evolution | the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems | Weizmannia coagulans |
evolution | the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems | Bacillus pumilus |
evolution | the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems | Citrobacter sp. |
evolution | the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems | Haemophilus aegyptius |
evolution | the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems | Acinetobacter lwoffii |
evolution | the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems | Campylobacter jejuni |
additional information | reaction mode of type IIB enzyme in one or two polypeptide systems, overview | Geobacillus stearothermophilus |
additional information | reaction mode of type IIB enzyme in one or two polypeptide systems, overview | Lysinibacillus sphaericus |
additional information | reaction mode of type IIB enzyme in one or two polypeptide systems, overview | Pseudomonas putida |
additional information | reaction mode of type IIB enzyme in one or two polypeptide systems, overview | Neisseria meningitidis |
additional information | reaction mode of type IIB enzyme in one or two polypeptide systems, overview | Weizmannia coagulans |
additional information | reaction mode of type IIB enzyme in one or two polypeptide systems, overview | Bacillus pumilus |
additional information | reaction mode of type IIB enzyme in one or two polypeptide systems, overview | Citrobacter sp. |
additional information | reaction mode of type IIB enzyme in one or two polypeptide systems, overview | Haemophilus aegyptius |
additional information | reaction mode of type IIB enzyme in one or two polypeptide systems, overview | Acinetobacter lwoffii |
additional information | reaction mode of type IIB enzyme in one or two polypeptide systems, overview | Campylobacter jejuni |
physiological function | the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex | Geobacillus stearothermophilus |
physiological function | the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex | Lysinibacillus sphaericus |
physiological function | the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex | Pseudomonas putida |
physiological function | the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex | Neisseria meningitidis |
physiological function | the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex | Weizmannia coagulans |
physiological function | the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex | Bacillus pumilus |
physiological function | the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex | Citrobacter sp. |
physiological function | the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex | Haemophilus aegyptius |
physiological function | the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex | Acinetobacter lwoffii |
physiological function | the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex | Campylobacter jejuni |