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Q9Z9H6 (RPOA_THETH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-directed RNA polymerase subunit alpha

Short name=RNAP subunit alpha
EC=2.7.7.6
Alternative name(s):
RNA polymerase subunit alpha
Transcriptase subunit alpha
Gene names
Name:rpoA
OrganismThermus thermophilus
Taxonomic identifier274 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. HAMAP-Rule MF_00059

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). HAMAP-Rule MF_00059

Subunit structure

Homodimer. 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.

Domain

The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements By similarity. HAMAP-Rule MF_00059

Sequence similarities

Belongs to the RNA polymerase alpha chain family.

Caution

The sequence shown here has been extracted from PDB entry 1IW7.

Ontologies

Keywords
   Biological processTranscription
   Cellular componentDNA-directed RNA polymerase
   Molecular functionNucleotidyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: InterPro

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

DNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 315315DNA-directed RNA polymerase subunit alpha HAMAP-Rule MF_00059
PRO_0000175409

Regions

Region1 – 229229Alpha N-terminal domain (alpha-NTD) HAMAP-Rule MF_00059
Region247 – 31569Alpha C-terminal domain (alpha-CTD) HAMAP-Rule MF_00059

Secondary structure

............................................... 315
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Z9H6 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: F79D93B57526A1CB

FASTA31535,013
        10         20         30         40         50         60 
MLDSKLKAPV FTVRTQGREY GEFVLEPLER GFGVTLGNPL RRILLSSIPG TAVTSVYIED 

        70         80         90        100        110        120 
VLHEFSTIPG VKEDVVEIIL NLKELVVRFL NPSLQTVTLL LKAEGPKEVK ARDFLPVADV 

       130        140        150        160        170        180 
EIMNPDLHIA TLEEGGRLNM EVRVDRGVGY VPAEKHGIKD RINAIPVDAV FSPVRRVAFQ 

       190        200        210        220        230        240 
VEDTRLGQRT DLDKLTLRIW TDGSVTPLEA LNQAVEILRE HLTYFSNPQA AAVAAPEEAK 

       250        260        270        280        290        300 
EPEAPPEQEE ELDLPLEELG LSTRVLHSLK EEGIESVRAL LALNLKDLKN IPGIGERSLE 

       310 
EIKEALEKKG FTLKE 

« Hide

References

[1]"The structure and the characteristic DNA binding property of the C-terminal domain of the RNA polymerase alpha subunit from Thermus thermophilus."
Wada T., Yamazaki T., Kyogoku Y.
J. Biol. Chem. 275:16057-16063(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 247-315.
[2]"Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution."
Vassylyev D.G., Sekine S., Laptenko O., Lee J., Vassylyeva M.N., Borukhov S., Yokoyama S.
Nature 417:712-719(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DOQNMR-A247-315[»]
1IW7X-ray2.60A/B/K/L1-315[»]
1SMYX-ray2.70A/B/K/L1-315[»]
2BE5X-ray2.40A/B/K/L1-315[»]
2PPBX-ray3.00A/B/K/L1-315[»]
3EQLX-ray2.70A/B/K/L1-315[»]
ProteinModelPortalQ9Z9H6.
SMRQ9Z9H6. Positions 1-229, 262-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60256N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.170.120.12. 1 hit.
HAMAPMF_00059. RNApol_bact_RpoA.
InterProIPR011262. DNA-dir_RNA_pol_insert.
IPR011263. DNA-dir_RNA_pol_RpoA/D/Rpb3.
IPR011773. DNA-dir_RpoA.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR009025. RBP11-like_dimer.
IPR011260. RNAP_asu_C.
[Graphical view]
PfamPF01000. RNA_pol_A_bac. 1 hit.
PF03118. RNA_pol_A_CTD. 1 hit.
PF01193. RNA_pol_L. 1 hit.
[Graphical view]
ProDomPD001179. RNAP_asu_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00278. HhH1. 1 hit.
SM00662. RPOLD. 1 hit.
[Graphical view]
SUPFAMSSF55257. SSF55257. 2 hits.
SSF56553. SSF56553. 1 hit.
TIGRFAMsTIGR02027. rpoA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9Z9H6.

Entry information

Entry nameRPOA_THETH
AccessionPrimary (citable) accession number: Q9Z9H6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references