Q9EVV4 (RPOZ_THEAQ) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 69.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: DNA-directed RNA polymerase subunit omega Short name=RNAP omega subunit EC=2.7.7.6 Alternative name(s): RNA polymerase omega subunit Transcriptase subunit omega | ||
| Gene names |
| ||
| Organism | Thermus aquaticus | ||
| Taxonomic identifier | 271 [NCBI] | ||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
Protein attributes
| Sequence length | 99 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. Ref.2 |
| Catalytic activity | Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). HAMAP MF_00366 |
| Subunit structure | The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription. |
| Sequence similarities | Belongs to the RNA polymerase subunit omega family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription |
| Cellular component | DNA-directed RNA polymerase |
| Molecular function | Nucleotidyltransferase Transferase |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | RNA polymerase complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | |||||||||||||||||||||||
| Chain | 2 – 99 | 98 | DNA-directed RNA polymerase subunit omega HAMAP MF_00366 | PRO_0000129002 | ||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||
| Helix | 6 – 11 | 6 | ||||||||||||||||||||||||
| Beta strand | 13 – 16 | 4 | ||||||||||||||||||||||||
| Helix | 17 – 32 | 16 | ||||||||||||||||||||||||
| Turn | 42 – 44 | 3 | ||||||||||||||||||||||||
| Beta strand | 51 – 53 | 3 | ||||||||||||||||||||||||
| Helix | 60 – 68 | 9 | ||||||||||||||||||||||||
| Turn | 69 – 71 | 3 | ||||||||||||||||||||||||
| Beta strand | 73 – 78 | 6 | ||||||||||||||||||||||||
| Helix | 82 – 85 | 4 | ||||||||||||||||||||||||
| Turn | 86 – 89 | 4 | ||||||||||||||||||||||||
Sequences
References
| [1] | "Recombinant Thermus aquaticus RNA polymerase, a new tool for structure-based analysis of transcription." Minakhin L., Nechaev S., Campbell E.A., Severinov K. J. Bacteriol. 183:71-76(2001) [PubMed: 11114902] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly." Minakhin L., Bhagat S., Brunning A., Campbell E.A., Darst S.A., Ebright R.H., Severinov K. Proc. Natl. Acad. Sci. U.S.A. 98:892-897(2001) [PubMed: 11158566] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, 3D-STRUCTURE MODELING. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AJ295839 Genomic DNA. Translation: CAC15848.1. | ||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||||||||||||||||||||
| ProteinModelPortal | Q9EVV4. | ||||||||||||||||||||||||||||||||||||||||||
| SMR | Q9EVV4. Positions 1-98. | ||||||||||||||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||||||||
| HAMAP | MF_00366. RNApol_bact_RpoZ. [Tree] | ||||||||||||||||||||||||||||||||||||||||||
| InterPro | IPR003716. DNA-dir_RNA_pol_omega. IPR006110. RNA_poly_omega/K/RPABC2. IPR012293. RNAP_RPB6_omega. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| Gene3D | G3DSA:3.90.940.10. RNAP_RPB6_omega. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||
| Pfam | PF01192. RNA_pol_Rpb6. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| SUPFAM | SSF63562. RNA_pol_omega. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||
| TIGRFAMs | TIGR00690. RpoZ. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||||||||||||||
Entry information
| Entry name | RPOZ_THEAQ | ||||||||
| Accession | Primary (citable) accession number: Q9EVV4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with