HRDCHelicase and RNase D C-terminal
|SMART accession number:||SM00341|
|Description:||Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.|
|Interpro abstract (IPR002121):|
The HRDC (helicase and RNaseD C-terminal) domain is comprised of two orthogonally packed alpha-hairpin subdomains, and is involved in interactions with DNA and protein.
HRDC domains are found at the C terminus of many RecQ helicases, including the human Werner and Bloom syndrome proteins [(PUBMED:10647186)]. RecQ helicases have been shown to unwind DNA in an ATP-dependent manner. The structure of the HRDC domain consists of a 4-5 helical bundle of two orthogonally packed alpha-hairpins, and as such it resembles auxiliary domains in bacterial DNA helicases and other proteins that interact with nucleic acids. A positively charged region on the surface of the HRDC domain is able to interact with DNA.
The HRDC domain has a putative role in nucleic acid binding. Mutations in the HRDC domain associated with the human BLM gene result in Bloom Syndrome (BS), an autosomal recessive disorder characterised by proportionate pre- and postnatal growth deficiency; sun-sensitive, telangiectatic, hypo- and hyperpigmented skin; predisposition to malignancy; and chromosomal instability [(PUBMED:9397680)].
|GO component:||intracellular (GO:0005622)|
|GO function:||nucleic acid binding (GO:0003676)|
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- Evolution (species in which this domain is found)
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