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Reviewed, UniProtKB/Swiss-Prot Q9KWU8 (RPOA_THEAQ)

Last modified September 22, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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):
    Transcriptase subunit alpha
    RNA polymerase subunit alpha
Gene names
Name: rpoA
OrganismThermus aquaticus
Taxonomic identifier271 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 MF_00059

Catalytic activity

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

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.

Sequence similarities

Belongs to the RNA polymerase alpha chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314DNA-directed RNA polymerase subunit alpha HAMAP MF_00059
PRO_0000175405

Regions

Region1 – 229229Alpha N-terminal domain (alpha-NTD) HAMAP MF_00059
Region246 – 31469Alpha C-terminal domain (alpha-CTD) HAMAP MF_00059

Secondary structure

........................................ 314
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9KWU8-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F2D0AB716619A3F0

FASTA31434,787
        10         20         30         40         50         60 
MLESKLKAPV FTATTQGDHY GEFVLEPLER GFGVTLGNPL RRILLSSIPG TAVTSVYIED 

        70         80         90        100        110        120 
VLHEFSTIPG VKEDVVEIIL NLKELVVRFL DPKMASTTLI LRAEGPKEVR AGDFTPSADV 

       130        140        150        160        170        180 
EIMNPDLHIA TLEEGGKLYM EVRVDRGVGY VPAERHGIKD RINAIPVDAI FSPVRRVAFQ 

       190        200        210        220        230        240 
VEDTRLGQRT DLDKLTLRIW TDGSVTPLEA LNQAVAILKE HLNYFANPEA SLLPTPEVSK 

       250        260        270        280        290        300 
GEKRESAEED LDLPLEELGL STRVLHSLKE EGIESVRALL ALNLKDLRNI PGIGERSLEE 

       310 
IRQALAKKGF TLKE 

« Hide

References

[1]"Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution."
Zhang G., Campbell E.A., Minakhin L., Richter C., Severinov K., Darst S.A.
Cell 98:811-824(1999) [PubMed: 10499798] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

Y19222 Genomic DNA. Translation: CAB65464.2.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1HQMX-ray3.30A/B1-314[»]
1I6VX-ray3.30A/B1-314[»]
1L9UX-ray4.00A/B/J/K1-314[»]
1L9ZX-ray6.50A/B1-314[»]
1YNJX-ray3.20A/B1-314[»]
1YNNX-ray3.30A/B1-314[»]
2GHOX-ray5.00A/B1-314[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.7.7.6. 118.

Family and domain databases

HAMAPMF_00059.
[Tree]
InterProIPR011261. DNA-dir_RNA_pol_dimersation.
IPR011262. DNA-dir_RNA_pol_insert.
IPR011263. DNA-dir_RNA_pol_RpoA/D/Rpb3.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR011260. RNAP_asu_C.
IPR011773. RpoA.
[Graphical view]
Gene3DG3DSA:2.170.120.12. RNAP_insert. 1 hit.
PfamPF01000. RNA_pol_A_bac. 1 hit.
PF03118. RNA_pol_A_CTD. 1 hit.
PF01193. RNA_pol_L. 1 hit.
[Graphical view]
ProDomPD001179. RNAP_alpha_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00278. HhH1. 1 hit.
SM00662. RPOLD. 1 hit.
[Graphical view]
TIGRFAMsTIGR02027. rpoA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRPOA_THEAQ
AccessionPrimary (citable) accession number: Q9KWU8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: September 22, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents