A0A0R2P3F1 · A0A0R2P3F1_9ACTN

Function

function

Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Features

Showing features for binding site.

153650100150200250300350400450500
TypeIDPosition(s)Description
Binding site275-280ATP (UniProtKB | ChEBI)
Binding site287-292ATP (UniProtKB | ChEBI)
Binding site318ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent activity, acting on RNA
Molecular Functionhelicase activity
Molecular FunctionRNA binding
Biological ProcessDNA-templated transcription termination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Transcription termination factor Rho
  • EC number
  • Alternative names
    • ATP-dependent helicase Rho

Gene names

    • Name
      rho
    • ORF names
      ABR64_00795

Organism names

Accessions

  • Primary accession
    A0A0R2P3F1

Proteomes

Interaction

Subunit

Homohexamer. The homohexamer assembles into an open ring structure.

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region54-146Disordered
Compositional bias55-81Basic and acidic residues
Compositional bias82-97Acidic residues
Compositional bias98-114Polar residues
Compositional bias115-146Basic and acidic residues
Domain157-232Rho RNA-BD

Sequence similarities

Belongs to the Rho family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    536
  • Mass (Da)
    59,423
  • Last updated
    2016-01-20 v1
  • Checksum
    324FB422588B8987
MAETSTRARRESGDLSALLLPELRKIATNLGIEGVADLKKPDLVTAITDLQAANREAAKAEREAKRAARNQKRRDNNSNETAPSDSEDDDQDEEDMPSDNSSNSSNNSSNGNSRDNSRGDREWRRDRHRDRGRDRSRDRDRPSRGEREIVLSEDDVLLPVGGLLDILDNYAFLRTAGYLPGPNDVYVSLQQVRKYGLRKGDVVTGQVRQAREGEKKEKFNALVRLDTINGMEPDSSKERVDFSKLVPLYPQDRLRLETLPNILTTRVIDLIAPIGKGQRGLIVSPPKAGKTMVLQAIANAITTNNPECHLMVVLVDERPEEVTDMQRSVKGEVIASTFDRPADDHTTVAELAIERAKRLVELGHDVVVLLDSITRLGRAYNIAAPASGRILSGGVDSAALYPPKKFFGAARNIEDGGSLTILATALVETGSKMDEVIFEEFKGTGNMELKLDRRFADKRIFPAVDIDASGTRKEEILMGPEELNIVWKLRRVLHALDSQQALELLLEKMKGTKSNAEFLMQVQKTTVGPDQSPKGE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias55-81Basic and acidic residues
Compositional bias82-97Acidic residues
Compositional bias98-114Polar residues
Compositional bias115-146Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LIAW01000077
EMBL· GenBank· DDBJ
KRO32598.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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