Any feedback?
Literature summary extracted from
- MicroRNA-independent roles of the RNase III enzymes Drosha and Dicer (2013), Open Biology, 3, 130144.
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.26.3 | additional information | Homo sapiens | Drosha recognizes the short internal stem-loop structure of long primary-microRNA transcript as part of a microprocessor complex and cleaves it at the base of the stem-loop, releasing it from the flanking single-stranded regions. Cleavage of both arms of the stem-loop is dependent on the tandem RNase III domains of Drosha binding and cleaving the dsRNA stem. The released stem-loop structure is exported from the nucleus by exportin 5 and is known as a pre-miRNA. Once in the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs. Drosha recognizes and cleaves stem-loop structures within the 50 end of the Dgcr8mRNA in mammalian cells, leading to destabilization of the mRNA. This cleavage therefore serves as a mechanism of gene repression, and is proposed to autoregulate the microprocessor complex | ? | - |
? |  |
| 3.1.26.3 | additional information | Drosophila melanogaster | Drosha recognizes the short internal stem-loop structure of long primary-microRNA transcript as part of a microprocessor complex and cleaves it at the base of the stem-loop, releasing it from the flanking single-stranded regions. Cleavage of both arms of the stem-loop is dependent on the tandem RNase III domains of Drosha binding and cleaving the dsRNA stem. The released stem-loop structure is exported from the nucleus by exportin 5 and is known as a pre-miRNA. Once in the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs. Drosha recognizes and cleaves stem-loop structures within the 50 end of the Dgcr8mRNA inmammalian cells, leading to destabilization of the mRNA. This cleavage therefore serves as amechanism of gene repression, and is proposed to autoregulate the microprocessor complex | ? | - |
? | |
| 3.1.26.3 | additional information | Mus musculus | In the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs | ? | - |
? | |
| 3.1.26.3 | additional information | Caenorhabditis elegans | In the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs | ? | - |
? | |
| 3.1.26.3 | additional information | Escherichia coli | the enzyme processes ribosomal RNA | ? | - |
? | |
| 3.1.26.3 | additional information | Saccharomyces cerevisiae | the enzyme processes ribosomal RNA, small nucleolar RNA, small nuclear RNA, and messenger RNA | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.26.3 | Arabidopsis thaliana | - |
- |
- |
| 3.1.26.3 | Caenorhabditis elegans | - |
- |
- |
| 3.1.26.3 | Drosophila melanogaster | - |
- |
- |
| 3.1.26.3 | Escherichia coli | - |
- |
- |
| 3.1.26.3 | Homo sapiens | - |
- |
- |
| 3.1.26.3 | Mus musculus | - |
- |
- |
| 3.1.26.3 | Saccharomyces cerevisiae | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.1.26.3 | HeLa cell | - |
Homo sapiens | - |
| 3.1.26.3 | additional information | the activity of Drosha is modulated between different cell types or differentiation stages | Drosophila melanogaster | - |
| 3.1.26.3 | additional information | the activity of Drosha is modulated between different cell types or differentiation stages | Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.26.3 | additional information | Drosha recognizes the short internal stem-loop structure of long primary-microRNA transcript as part of a microprocessor complex and cleaves it at the base of the stem-loop, releasing it from the flanking single-stranded regions. Cleavage of both arms of the stem-loop is dependent on the tandem RNase III domains of Drosha binding and cleaving the dsRNA stem. The released stem-loop structure is exported from the nucleus by exportin 5 and is known as a pre-miRNA. Once in the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs. Drosha recognizes and cleaves stem-loop structures within the 50 end of the Dgcr8mRNA in mammalian cells, leading to destabilization of the mRNA. This cleavage therefore serves as a mechanism of gene repression, and is proposed to autoregulate the microprocessor complex | Homo sapiens | ? | - |
? | |
| 3.1.26.3 | additional information | Drosha recognizes the short internal stem-loop structure of long primary-microRNA transcript as part of a microprocessor complex and cleaves it at the base of the stem-loop, releasing it from the flanking single-stranded regions. Cleavage of both arms of the stem-loop is dependent on the tandem RNase III domains of Drosha binding and cleaving the dsRNA stem. The released stem-loop structure is exported from the nucleus by exportin 5 and is known as a pre-miRNA. Once in the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs. Drosha recognizes and cleaves stem-loop structures within the 50 end of the Dgcr8mRNA inmammalian cells, leading to destabilization of the mRNA. This cleavage therefore serves as amechanism of gene repression, and is proposed to autoregulate the microprocessor complex | Drosophila melanogaster | ? | - |
? | |
| 3.1.26.3 | additional information | In the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs | Mus musculus | ? | - |
? | |
| 3.1.26.3 | additional information | In the cytoplasm the pre-miRNA is cleaved by Dicer, in complex with another dsRNA-binding protein, Trbp. The PAZ domain of Dicer binds the basal end of the double-stranded pre-miRNA, and guides the stem into a cleft formed by the intramolecular dimerization of two RNase III domains. Scission of the RNA removes the loop structure, leaving a miRNA duplex. The distance from the PAZ domain to the RNase III domain dimer is thought to define the length of the RNA product, typically approximately 22 nt for miRNAs | Caenorhabditis elegans | ? | - |
? | |
| 3.1.26.3 | additional information | the enzyme processes ribosomal RNA | Escherichia coli | ? | - |
? | |
| 3.1.26.3 | additional information | the enzyme processes ribosomal RNA, small nucleolar RNA, small nuclear RNA, and messenger RNA | Saccharomyces cerevisiae | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.26.3 | More | domain structure: the enzyme Dicer is composed of helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain, comparison of class I-III enzymes, overview | Mus musculus |
| 3.1.26.3 | More | domain structure: the enzyme Dicer is composed of helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain, while enzyme Drosha is composed of P-rich domain, RS-rich domain, two RNase III domains, and dsRNA binding domain, comparison of class I-III enzymes, overview | Homo sapiens |
| 3.1.26.3 | More | domain structure: the enzyme is composed of helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain, comparison of class I-III enzymes, overview | Caenorhabditis elegans |
| 3.1.26.3 | More | domain structure: the enzyme is composed of N-terminal domain, RNase III domain and dsRNA binding domain, comparison of class I-III enzymes, overview | Saccharomyces cerevisiae |
| 3.1.26.3 | More | domain structure: the enzyme is composed of RNase III domain and dsRNA binding domain, comparison of class I-III enzymes, overview | Escherichia coli |
| 3.1.26.3 | More | domain structures of isozymes DCL1-4 are all composed of helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain, only CL-1 shows a double dsRNA binding domain and DCL3 lacks the N-terminal domain. Comparison of class I-III enzymes, overview | Arabidopsis thaliana |
| 3.1.26.3 | More | domain structures: the enzyme Drosha is composed of P-rich domain, two RNase III domains, and dsRNA binding domain. The enzyme Dicer-1 is composed of truncated helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain, and enzyme Dicer-2 is composed of helicase domain, N-terminal domain, PAZ domain, two RNase III domains, and dsRNA binding domain. Comparison of class I-III enzymes, overview | Drosophila melanogaster |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.26.3 | DCL1 | - |
Arabidopsis thaliana |
| 3.1.26.3 | DCL2 | - |
Arabidopsis thaliana |
| 3.1.26.3 | DCL3 | - |
Arabidopsis thaliana |
| 3.1.26.3 | DCL4 | - |
Arabidopsis thaliana |
| 3.1.26.3 | Dicer | - |
Mus musculus |
| 3.1.26.3 | Dicer | - |
Homo sapiens |
| 3.1.26.3 | Dicer | - |
Caenorhabditis elegans |
| 3.1.26.3 | Dicer-1 | - |
Drosophila melanogaster |
| 3.1.26.3 | Dicer-2 | - |
Drosophila melanogaster |
| 3.1.26.3 | Drosha | - |
Drosophila melanogaster |
| 3.1.26.3 | Drosha | - |
Homo sapiens |
| 3.1.26.3 | RNase III | - |
Drosophila melanogaster |
| 3.1.26.3 | RNase III | - |
Escherichia coli |
| 3.1.26.3 | RNase III | - |
Saccharomyces cerevisiae |
| 3.1.26.3 | RNT1 | - |
Saccharomyces cerevisiae |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.26.3 | evolution | class I enzymes are the simplest, consisting of those found in bacteria and simple eukaryotes, such as RNase III in Escherichia coli. These are thought to be the antecedents of the more complex class II Drosha and class III Dicer proteins. Class I enzymes achieve the dimeric catalytic RNase III module by forming dimers, whereas the more complex class II and III members use intramolecular dimerization of their two RNase III domains | Escherichia coli |
| 3.1.26.3 | evolution | class I enzymes are the simplest, consisting of those found in bacteria and simple eukaryotes, such as Rnt1 in Saccharomyces cerevisiae. These are thought to be the antecedents of the more complex class II Drosha and class III Dicer proteins. Class I enzymes achieve the dimeric catalytic RNase III module by forming dimers, whereas the more complex class II and III members use intramolecular dimerization of their two RNase III domains | Drosophila melanogaster |
| 3.1.26.3 | evolution | class I enzymes are the simplest, consisting of those found in bacteria and simple eukaryotes, such as Rnt1 in Saccharomyces cerevisiae. These are thought to be the antecedents of the more complex class II Drosha and class III Dicer proteins. Class I enzymes achieve the dimeric catalytic RNase III module by forming dimers, whereas the more complex class II and III members use intramolecular dimerization of their two RNase III domains | Mus musculus |
| 3.1.26.3 | evolution | class I enzymes are the simplest, consisting of those found in bacteria and simple eukaryotes, such as Rnt1 in Saccharomyces cerevisiae. These are thought to be the antecedents of the more complex class II Drosha and class III Dicer proteins. Class I enzymes achieve the dimeric catalytic RNase III module by forming dimers, whereas the more complex class II and III members use intramolecular dimerization of their two RNase III domains | Homo sapiens |
| 3.1.26.3 | evolution | class I enzymes are the simplest, consisting of those found in bacteria and simple eukaryotes, such as Rnt1 in Saccharomyces cerevisiae. These are thought to be the antecedents of the more complex class II Drosha and class III Dicer proteins. Class I enzymes achieve the dimeric catalytic RNase III module by forming dimers, whereas the more complex class II and III members use intramolecular dimerization of their two RNase III domains | Saccharomyces cerevisiae |
| 3.1.26.3 | evolution | class I enzymes are the simplest, consisting of those found in bacteria and simple eukaryotes, such as Rnt1 in Saccharomyces cerevisiae. These are thought to be the antecedents of the more complex class II Drosha and class III Dicer proteins. Class I enzymes achieve the dimeric catalytic RNase III module by forming dimers, whereas the more complex class II and III members use intramolecular dimerization of their two RNase III domains | Arabidopsis thaliana |
| 3.1.26.3 | evolution | class I enzymes are the simplest, consisting of those found in bacteria and simple eukaryotes, such as Rnt1 in Saccharomyces cerevisiae. These are thought to be the antecedents of the more complex class II Drosha and class III Dicer proteins. Class I enzymes achieve the dimeric catalytic RNase III module by forming dimers, whereas the more complex class II and III members use intramolecular dimerization of their two RNase III domains | Caenorhabditis elegans |
| 3.1.26.3 | malfunction | Drosha knockdown, but not Dicer knockdown, in stromal cells leads to a partial stall in the G1 phase of the cell cycle. In the absence of regulation by Drosha, neurogenin 2, Ngn2, accumulates resulting in a loss of stem cell fidelity and ultimately neuronal degeneration, the phenotype is independent of miRNAs. Non-redundant phenotypes caused by Drosha or Dicer deficiency occur most commonly in progenitor populations as opposed to mature, differentiated cell types. Knockdown of either Drosha or Dicer in human cells permits aberrant DNA replication and cell division in DNAdamage-induced senescent cells | Homo sapiens |
| 3.1.26.3 | malfunction | Drosha knockdown, but not Dicer knockdown, in stromal cells led to a partial stall in the G1 phase of the cell cycle. In the absence of regulation by Drosha, neurogenin 2, Ngn2, accumulates resulting in a loss of stem cell fidelity and ultimately neuronal degeneration, the phenotype is independent of miRNAs. Non-redundant phenotypes caused by Drosha or Dicer deficiency occur most commonly in progenitor populations as opposed to mature, differentiated cell types | Drosophila melanogaster |
| 3.1.26.3 | malfunction | non-redundant phenotypes caused by Dicer deficiency occur most commonly in progenitor populations as opposed to mature, differentiated cell types | Mus musculus |
| 3.1.26.3 | malfunction | non-redundant phenotypes caused by Dicer deficiency occur most commonly in progenitor populations as opposed to mature, differentiated cell types | Caenorhabditis elegans |
| 3.1.26.3 | physiological function | the ribonuclease III enzyme Dicer has a central role in the biogenesis of microRNAs and small interfering RNAs. Dicer also acts in the biogenesis of DNA-damage-associated small RNAs, overview. Additionally, Dicer has critical roles in genome regulation and surveillance, including the production of endogenous small interfering RNAs from many sources, and the degradation of potentially harmful short interspersed element and viral RNAs | Mus musculus |
| 3.1.26.3 | physiological function | the ribonuclease III enzyme Dicer has a central role in the biogenesis of microRNAs and small interfering RNAs. Dicer also acts in the biogenesis of DNA-damage-associated small RNAs, overview. Additionally, Dicer has critical roles in genome regulation and surveillance, including the production of endogenous small interfering RNAs from many sources, and the degradation of potentially harmful short interspersed element and viral RNAs | Caenorhabditis elegans |
| 3.1.26.3 | physiological function | the ribonuclease III enzymes Drosha and Dicer have central roles in the biogenesis of ribosomal RNA, microRNAs and small interfering RNAs, including p53, Lin28, DEAD-box RNA helicases and Smads. In neuronal progenitors, Drosha normally binds and cleaves stem-loop structures within the 3' UTR of proneuronal transcription factor neurogenin 2, Ngn2. Drosha also recognizes and cleaves messenger RNAs, and Drosha is necessary for the maturation of ribosomal RNA. mRNA cleavage occurs via recognition of secondary stem-loop structures similar to miRNA precursors, and is an important mechanism of repressing gene expression, particularly in progenitor/stem cell populations. Drosha-mediated rRNA processing is implicated in regulating cell cycle progression in human multi-potent stromal cells. Drosha and Dicer act in the biogenesis of DNA-damage-associated small RNAs, overview. Dicer also has critical roles in genome regulation and surveillance, including the production of endogenous small interfering RNAs from many sources, and the degradation of potentially harmful short interspersed element and viral RNAs | Homo sapiens |
| 3.1.26.3 | physiological function | the ribonuclease III enzymes Drosha and Dicer have central roles in the biogenesis of ribosomal RNA, microRNAs and small interfering RNAs, including p53, Lin28, DEAD-box RNA helicases and Smads. In neuronal progenitors, Drosha normally binds and cleaves stem-loop structures within the 3' UTR of proneuronal transcription factor neurogenin 2, Ngn2. Drosha also recognizes and cleaves messenger RNAs, and is necessary for the maturation of rRNA. mRNA cleavage occurs via recognition of secondary stem-loop structures similar to miRNA precursors, and is an important mechanism of repressing gene expression, particularly in progenitor/stem cell populations. Drosha and Dicer act in the biogenesis of DNA-damage-associated small RNAs, overview. Dicer also has critical roles in genome regulation and surveillance, including the production of endogenous small interfering RNAs from many sources, and the degradation of potentially harmful short interspersed element and viral RNAs | Drosophila melanogaster |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
