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Q9Z9H6

- RPOA_THETH

UniProt

Q9Z9H6 - RPOA_THETH

Protein

DNA-directed RNA polymerase subunit alpha

Gene

rpoA

Organism
Thermus thermophilus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-HAMAP
    2. DNA-directed RNA polymerase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. DNA repair Source: InterPro
    2. transcription, DNA-templated Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Transcription

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA-directed RNA polymerase subunit alpha (EC:2.7.7.6)
    Short name:
    RNAP subunit alpha
    Alternative name(s):
    RNA polymerase subunit alpha
    Transcriptase subunit alpha
    Gene namesi
    Name:rpoA
    OrganismiThermus thermophilus
    Taxonomic identifieri274 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

    Subcellular locationi

    Keywords - Cellular componenti

    DNA-directed RNA polymerase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 315315DNA-directed RNA polymerase subunit alphaPRO_0000175409Add
    BLAST

    Interactioni

    Subunit structurei

    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.

    Protein-protein interaction databases

    DIPiDIP-60256N.

    Structurei

    Secondary structure

    1
    315
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Beta strandi10 – 167
    Turni17 – 193
    Beta strandi20 – 289
    Helixi32 – 4615
    Beta strandi48 – 6013
    Beta strandi71 – 744
    Helixi75 – 839
    Beta strandi87 – 893
    Beta strandi95 – 10612
    Beta strandi108 – 1103
    Helixi111 – 1133
    Beta strandi118 – 1236
    Beta strandi128 – 1325
    Beta strandi137 – 15115
    Helixi153 – 1564
    Beta strandi173 – 1819
    Beta strandi193 – 2019
    Beta strandi203 – 2053
    Helixi207 – 22317
    Helixi256 – 2594
    Helixi263 – 2719
    Helixi277 – 2826
    Helixi285 – 2884
    Helixi296 – 30914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ9Z9H6.
    SMRiQ9Z9H6. Positions 1-229, 262-315.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Z9H6.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 229229Alpha N-terminal domain (alpha-NTD)Add
    BLAST
    Regioni247 – 31569Alpha C-terminal domain (alpha-CTD)Add
    BLAST

    Domaini

    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 similaritiesi

    Belongs to the RNA polymerase alpha chain family.Curated

    Family and domain databases

    Gene3Di2.170.120.12. 1 hit.
    HAMAPiMF_00059. RNApol_bact_RpoA.
    InterProiIPR011262. 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]
    PfamiPF01000. RNA_pol_A_bac. 1 hit.
    PF03118. RNA_pol_A_CTD. 1 hit.
    PF01193. RNA_pol_L. 1 hit.
    [Graphical view]
    ProDomiPD001179. RNAP_asu_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00278. HhH1. 1 hit.
    SM00662. RPOLD. 1 hit.
    [Graphical view]
    SUPFAMiSSF55257. SSF55257. 2 hits.
    SSF56553. SSF56553. 1 hit.
    TIGRFAMsiTIGR02027. rpoA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9Z9H6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLDSKLKAPV FTVRTQGREY GEFVLEPLER GFGVTLGNPL RRILLSSIPG    50
    TAVTSVYIED VLHEFSTIPG VKEDVVEIIL NLKELVVRFL NPSLQTVTLL 100
    LKAEGPKEVK ARDFLPVADV EIMNPDLHIA TLEEGGRLNM EVRVDRGVGY 150
    VPAEKHGIKD RINAIPVDAV FSPVRRVAFQ VEDTRLGQRT DLDKLTLRIW 200
    TDGSVTPLEA LNQAVEILRE HLTYFSNPQA AAVAAPEEAK EPEAPPEQEE 250
    ELDLPLEELG LSTRVLHSLK EEGIESVRAL LALNLKDLKN IPGIGERSLE 300
    EIKEALEKKG FTLKE 315
    Length:315
    Mass (Da):35,013
    Last modified:May 1, 1999 - v1
    Checksum:iF79D93B57526A1CB
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DOQ NMR - A 247-315 [» ]
    1IW7 X-ray 2.60 A/B/K/L 1-315 [» ]
    1SMY X-ray 2.70 A/B/K/L 1-315 [» ]
    2BE5 X-ray 2.40 A/B/K/L 1-315 [» ]
    2PPB X-ray 3.00 A/B/K/L 1-315 [» ]
    3EQL X-ray 2.70 A/B/K/L 1-315 [» ]
    ProteinModelPortali Q9Z9H6.
    SMRi Q9Z9H6. Positions 1-229, 262-315.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60256N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q9Z9H6.

    Family and domain databases

    Gene3Di 2.170.120.12. 1 hit.
    HAMAPi MF_00059. RNApol_bact_RpoA.
    InterProi IPR011262. 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 ]
    Pfami PF01000. RNA_pol_A_bac. 1 hit.
    PF03118. RNA_pol_A_CTD. 1 hit.
    PF01193. RNA_pol_L. 1 hit.
    [Graphical view ]
    ProDomi PD001179. RNAP_asu_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00278. HhH1. 1 hit.
    SM00662. RPOLD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55257. SSF55257. 2 hits.
    SSF56553. SSF56553. 1 hit.
    TIGRFAMsi TIGR02027. rpoA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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).

    Entry informationi

    Entry nameiRPOA_THETH
    AccessioniPrimary (citable) accession number: Q9Z9H6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

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

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3