Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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RQC

SMART accession number:	SM00956
Description:	This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain (PUBMED:16530788).
Interpro abstract (IPR018982):	This entry represents the RQC domain, which is a DNA-binding domain found only in RecQ family enzymes. RecQ family helicases can unwind G4 DNA, and play important roles at G-rich domains of the genome, including the telomeres, rDNA, and immunoglobulin switch regions. This domain has a helix-turn-helix structure and acts as a high affinity G4 DNA binding domain [(PUBMED:16530788)]. Binding of RecQ to Holliday junctions involves both the RQC and the HRDC domains.
GO process:	DNA repair (GO:0006281), DNA replication (GO:0006260)
GO function:	ATP-dependent 3'-5' DNA helicase activity (GO:0043140)
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 1332 RQC domains in 1332 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a RQC domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with RQC domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae

• Cellular role (predicted cellular role)

• Cellular role: chromatin
  Binding / catalysis: DNA-binding

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Huber MD, Duquette ML, Shiels JC, Maizels N
  • A conserved G4 DNA binding domain in RecQ family helicases.
  • J Mol Biol. 2006; 358: 1071-80
  • Display abstract

  • RecQ family helicases play important roles at G-rich domains of thegenome, including the telomeres, rDNA, and immunoglobulin switch regions.This appears to reflect the unusual ability of enzymes in this family tounwind G4 DNA. How RecQ family helicases recognize this substrate has notbeen established. Here, we show that G4 DNA is a preferred target for BLMhelicase within the context of long DNA molecules. We identify the RQCdomain, found only in RecQ family enzymes, as an independent, highaffinity and conserved G4 DNA binding domain; and show that binding toHolliday junctions involves both the RQC and the HRDC domains. Theseresults provide mechanistic understanding of differences and redundanciesof function and activities among RecQ family helicases, and of howdeficiencies in human members of this family may contribute to genomicinstability and disease.

• Structure (3D structures containing this domain)

• 3D Structures of RQC domains in PDB

  PDB code	Main view	Title
  1oyw		Structure of the recq catalytic core
  1oyy		Structure of the recq catalytic core bound to atp-gamma-s
  2axl		Solution structure of a multifunctional dna- and protein- binding domain of human werner syndrome protein

• Links (links to other resources describing this domain)

• PFAM	RQC
  INTERPRO	IPR018982

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