A0A059GBG5 · A0A059GBG5_9PROT
- ProteinRibonuclease E
- Generne
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids887 (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 | 387 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 430 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 488 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 491 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomonadales > Hyphomonadaceae > Hyphomonas
Accessions
- Primary accessionA0A059GBG5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Interaction
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 38-203 | S1 motif | ||||
Sequence: LRGNIYLAKVTRVEPSLQAAFVEYGGNRHGFLAFSEIHPDYYQLPAEDREALLKEAAEEAAAQIEDEDDDDIEGDEDAHADADDSDDSDDDASDDDEDDGDDESEDGESKASAKPARGRRPARKESPRSSISKRYKIQEVIRRRQVMLVQVVKEERGNKGAALTTF | ||||||
Region | 96-172 | Disordered | ||||
Sequence: EAAAQIEDEDDDDIEGDEDAHADADDSDDSDDDASDDDEDDGDDESEDGESKASAKPARGRRPARKESPRSSISKRY | ||||||
Compositional bias | 98-143 | Acidic residues | ||||
Sequence: AAQIEDEDDDDIEGDEDAHADADDSDDSDDDASDDDEDDGDDESED | ||||||
Compositional bias | 144-172 | Basic and acidic residues | ||||
Sequence: GESKASAKPARGRRPARKESPRSSISKRY | ||||||
Region | 488-491 | Required for zinc-mediated homotetramerization and catalytic activity | ||||
Sequence: CEAC | ||||||
Compositional bias | 567-581 | Basic and acidic residues | ||||
Sequence: FMIDAERDPNSKPKK | ||||||
Region | 567-887 | Disordered | ||||
Sequence: FMIDAERDPNSKPKKKSPPRSLSKSTKPAVSDEDDDEDIEDEDDEAVAETDDEAEDKAEDTQGKPRKRRRRRGGRGRNRDARDTGLEVIDGETAPAAASSDDDSDDDADDEGEGGNAPEARSDDSEEAGRKRRRRGRRGGRRRRRSGGEDRAEGAQEGAPTDGGAYLDGLSASAPEMLDAEAPSDAKPEEAPAPATEASEPAPAKAAEVEADTDTDEPVKAEKPKRARRSRAKPKPEAEAPAAEAAPAPVETKAAPEPKAEPKPAPDVTPAPVVEAVKETVAAEAAPAPEPKPEPKPEPAKAEAKDTGTKRKGWWARARGE | ||||||
Compositional bias | 598-622 | Acidic residues | ||||
Sequence: DEDDDEDIEDEDDEAVAETDDEAED | ||||||
Compositional bias | 665-679 | Acidic residues | ||||
Sequence: SSDDDSDDDADDEGE | ||||||
Compositional bias | 680-697 | Basic and acidic residues | ||||
Sequence: GGNAPEARSDDSEEAGRK | ||||||
Compositional bias | 773-790 | Basic and acidic residues | ||||
Sequence: AEVEADTDTDEPVKAEKP | ||||||
Compositional bias | 860-887 | Basic and acidic residues | ||||
Sequence: EPKPEPAKAEAKDTGTKRKGWWARARGE |
Sequence similarities
Belongs to the RNase E/G family. RNase E subfamily.
Belongs to the RNase E/G family. RNase G subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length887
- Mass (Da)96,924
- Last updated2014-07-09 v1
- Checksum32E6D78D983676C9
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 98-143 | Acidic residues | ||||
Sequence: AAQIEDEDDDDIEGDEDAHADADDSDDSDDDASDDDEDDGDDESED | ||||||
Compositional bias | 144-172 | Basic and acidic residues | ||||
Sequence: GESKASAKPARGRRPARKESPRSSISKRY | ||||||
Compositional bias | 567-581 | Basic and acidic residues | ||||
Sequence: FMIDAERDPNSKPKK | ||||||
Compositional bias | 598-622 | Acidic residues | ||||
Sequence: DEDDDEDIEDEDDEAVAETDDEAED | ||||||
Compositional bias | 665-679 | Acidic residues | ||||
Sequence: SSDDDSDDDADDEGE | ||||||
Compositional bias | 680-697 | Basic and acidic residues | ||||
Sequence: GGNAPEARSDDSEEAGRK | ||||||
Compositional bias | 773-790 | Basic and acidic residues | ||||
Sequence: AEVEADTDTDEPVKAEKP | ||||||
Compositional bias | 860-887 | Basic and acidic residues | ||||
Sequence: EPKPEPAKAEAKDTGTKRKGWWARARGE |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ARYL01000002 EMBL· GenBank· DDBJ | KDA04079.1 EMBL· GenBank· DDBJ | Genomic DNA |