A0A0A2B7M7 · A0A0A2B7M7_PROMR
- ProteinDNA-directed RNA polymerase subunit beta'
- GenerpoC2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1340 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic activity
- RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
Cofactor
Note: Binds 1 Zn2+ ion per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | DNA-directed RNA polymerase complex | |
Molecular Function | DNA binding | |
Molecular Function | DNA-directed 5'-3' RNA polymerase activity | |
Molecular Function | zinc ion binding | |
Biological Process | DNA-templated transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA-directed RNA polymerase subunit beta'
- EC number
- Short namesRNAP subunit beta'
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Synechococcales > Prochlorococcaceae > Prochlorococcus
Accessions
- Primary accessionA0A0A2B7M7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Interaction
Subunit
In cyanobacteria the RNAP catalytic core is composed of 2 alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-64 | RNA polymerase Rpb1 | ||||
Sequence: FKNKVVDKKALKNLVSWAYKTHGTAITAAMADNLKDLGFKYATQAAVSISVDDL | ||||||
Domain | 93-171 | RNA polymerase Rpb1 | ||||
Sequence: ITEVERHTKVIDTWTETNERLVDAVKNNFNQNDPLNSVWMMANSGARGNMSQVRQLVGMRGLMANPQGEIIDLPIRTNF | ||||||
Domain | 174-372 | RNA polymerase Rpb1 | ||||
Sequence: GLTVTEYVISSYGARKGLVDTALRTADSGYLTRRLVDVAQDVIVREEDCGTERSIVVAAEDGKFGARLLGRLTAEDIFDAEENLVVPQNTAIDPALSGEIEKASISEVKIRSPLTCEANRSVCRRCYGWALAHNHLVDLGEAVGIIAAQSIGEPGTQLTMRTFHTGGVSTAESGVVRSKISGKFEFSSKAKVRGYRTPH | ||||||
Domain | 1092-1182 | RNA polymerase Rpb1 | ||||
Sequence: SISKLQRSMVSEVQNVYKSQGVAIDDKHIEVIVRQMTSKVRIEDAGDTTLLPGELIELRQVEDTNQAMAITGGAPAEFTPVLLGITKASLN | ||||||
Region | 1266-1340 | Disordered | ||||
Sequence: TVDMPQSPAVSSTAILDDPSDEDLETTRSRHGIDPTSSNFAAFARPNAENQFSEDQLPDPAALEGLQEEGLLSDE | ||||||
Compositional bias | 1296-1319 | Polar residues | ||||
Sequence: HGIDPTSSNFAAFARPNAENQFSE |
Sequence similarities
Belongs to the RNA polymerase beta' chain family. RpoC2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,340
- Mass (Da)146,429
- Last updated2015-02-04 v1
- ChecksumBA9E3583CADCF8F1
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1296-1319 | Polar residues | ||||
Sequence: HGIDPTSSNFAAFARPNAENQFSE |