A0A1E2UV46 · A0A1E2UV46_9GAMM
- ProteinRibonuclease E
- Generne
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1001 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
Catalytic activity
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mg2+ ion per subunit.
Note: Binds 2 Zn2+ ions per homotetramer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 299 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 342 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 400 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 403 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic side of plasma membrane | |
Molecular Function | magnesium ion binding | |
Molecular Function | ribonuclease E activity | |
Molecular Function | RNA endonuclease activity | |
Molecular Function | rRNA binding | |
Molecular Function | tRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | mRNA catabolic process | |
Biological Process | rRNA processing | |
Biological Process | tRNA processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibonuclease E
- EC number
- Short namesRNase E
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Chromatiales > Sedimenticolaceae > Candidatus Thiodiazotropha
Accessions
- Primary accessionA0A1E2UV46
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Interaction
Subunit
Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Within the RNA degradosome, RNase E assembles into a homotetramer formed by a dimer of dimers.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 36-117 | S1 motif | ||||
Sequence: ANIYKGRITRVEPSLEAAFVDYGAERHGFLPLKEISRSYFTNKARESSGRVNIQEALKEGQEVIVQVEKEERGNKGAALTTF | ||||||
Region | 400-403 | Required for zinc-mediated homotetramerization and catalytic activity | ||||
Sequence: CPRC | ||||||
Region | 518-556 | Disordered | ||||
Sequence: VKSEQPAVKSIAPASPAPQRAEAPAPTPAPAATDSQTGE | ||||||
Region | 571-1001 | Disordered | ||||
Sequence: EAEPVQPEAEEKKAPARQQSGSNSNNRRGRRAAQPGGRNVKSAGGERRGDNRNQDKPSNRRRGGNKAGGSADKRATQEKKPQEQAAPATAAAAGDNTETTTKPKSRRGRRGGRRRRSAAERNNEQTTVNNGATEATSEAPAQEKSQEKSQEKPKRQQPRAQKKPASPRAAKVETSTEAKQETESRDDNSRVEAKQKPQQVDRVAERAEAGPKEKPKAKPQPEQQAKSAQSEPATAKPVESQASSESKPEAGLKPAKKRETTTAESKPSEQKAKPAKPAGQVETTKAKTEIKEKPAETKATQTSARKEPVENAVKPKPKPKPKPKAVKLQQVETKPIAQESKAESAKVEKPKTNATAETQIAKAEAKATPESQAAKPEARATPRPQAAKPEARATIEKAQESRAQPASKTVQVETKKPAANTDVKVADASGD | ||||||
Compositional bias | 586-600 | Polar residues | ||||
Sequence: ARQQSGSNSNNRRGR | ||||||
Compositional bias | 613-650 | Basic and acidic residues | ||||
Sequence: AGGERRGDNRNQDKPSNRRRGGNKAGGSADKRATQEKK | ||||||
Compositional bias | 692-713 | Polar residues | ||||
Sequence: NNEQTTVNNGATEATSEAPAQE | ||||||
Compositional bias | 714-728 | Basic and acidic residues | ||||
Sequence: KSQEKSQEKPKRQQP | ||||||
Compositional bias | 744-790 | Basic and acidic residues | ||||
Sequence: TSTEAKQETESRDDNSRVEAKQKPQQVDRVAERAEAGPKEKPKAKPQ | ||||||
Compositional bias | 792-817 | Polar residues | ||||
Sequence: EQQAKSAQSEPATAKPVESQASSESK | ||||||
Compositional bias | 820-841 | Basic and acidic residues | ||||
Sequence: AGLKPAKKRETTTAESKPSEQK | ||||||
Compositional bias | 855-870 | Basic and acidic residues | ||||
Sequence: KAKTEIKEKPAETKAT | ||||||
Compositional bias | 970-986 | Polar residues | ||||
Sequence: ESRAQPASKTVQVETKK |
Sequence similarities
Belongs to the RNase E/G family. RNase E subfamily.
Belongs to the RNase E/G family. RNase G subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,001
- Mass (Da)110,202
- Last updated2017-01-18 v1
- ChecksumE9C4340C2073376A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 586-600 | Polar residues | ||||
Sequence: ARQQSGSNSNNRRGR | ||||||
Compositional bias | 613-650 | Basic and acidic residues | ||||
Sequence: AGGERRGDNRNQDKPSNRRRGGNKAGGSADKRATQEKK | ||||||
Compositional bias | 692-713 | Polar residues | ||||
Sequence: NNEQTTVNNGATEATSEAPAQE | ||||||
Compositional bias | 714-728 | Basic and acidic residues | ||||
Sequence: KSQEKSQEKPKRQQP | ||||||
Compositional bias | 744-790 | Basic and acidic residues | ||||
Sequence: TSTEAKQETESRDDNSRVEAKQKPQQVDRVAERAEAGPKEKPKAKPQ | ||||||
Compositional bias | 792-817 | Polar residues | ||||
Sequence: EQQAKSAQSEPATAKPVESQASSESK | ||||||
Compositional bias | 820-841 | Basic and acidic residues | ||||
Sequence: AGLKPAKKRETTTAESKPSEQK | ||||||
Compositional bias | 855-870 | Basic and acidic residues | ||||
Sequence: KAKTEIKEKPAETKAT | ||||||
Compositional bias | 970-986 | Polar residues | ||||
Sequence: ESRAQPASKTVQVETKK |
Keywords
- Technical term