The domain within your query sequence starts at position 1 and ends at position 83; the E-value for the XPGN domain shown below is 3.5e-11.



Xeroderma pigmentosum G N-region
SMART accession number:SM00485
Description: domain in nucleases
Interpro abstract (IPR006085):

Xeroderma pigmentosum (XP) [ (PUBMED:8160271) ] is a human autosomal recessive disease, characterised by a high incidence of sunlight-induced skin cancer. People's skin cells with this condition are hypersensitive to ultraviolet light, due to defects in the incision step of DNA excision repair. There are a minimum of seven genetic complementation groups involved in this pathway: XP-A to XP-G. XP-G is one of the most rare and phenotypically heterogeneous of XP, showing anything from slight to extreme dysfunction in DNA excision repair [ (PUBMED:8464724) (PUBMED:8206890) ]. XP-G can be corrected by a 133 Kd nuclear protein, XPGC [ (PUBMED:8160271) ]. XPGC is an acidic protein that confers normal UV resistance in expressing cells [ (PUBMED:8206890) ]. It is a magnesium-dependent, single-strand DNA endonuclease that makes structure-specific endonucleolytic incisions in a DNA substrate containing a duplex region and single-stranded arms [ (PUBMED:8206890) (PUBMED:8090225) ]. XPGC cleaves one strand of the duplex at the border with the single-stranded region [ (PUBMED:8090225) ].

XPG belongs to a family of proteins that includes RAD2 from Saccharomyces cerevisiae (Baker's yeast) and rad13 from Schizosaccharomyces pombe (Fission yeast), which are single-stranded DNA endonucleases [ (PUBMED:8090225) (PUBMED:8247134) ]; mouse and human FEN-1, a structure-specific endonuclease; RAD2 from fission yeast and RAD27 from budding yeast; fission yeast exo1, a 5'-3' double-stranded DNA exonuclease that may act in a pathway that corrects mismatched base pairs; yeast DHS1, and yeast DIN7. Sequence alignment of this family of proteins reveals that similarities are largely confined to two regions. The first is located at the N-terminal extremity (N-region) and corresponds to the first 95 to 105 amino acids. The second region is internal (I-region) and found towards the C terminus; it spans about 140 residues and contains a highly conserved core of 27 amino acids that includes a conserved pentapeptide (E-A-[DE]-A-[QS]). It is possible that the conserved acidic residues are involved in the catalytic mechanism of DNA excision repair in XPG. The amino acids linking the N- and I-regions are not conserved.

This entry represents the N-terminal of XPG.

GO function:nuclease activity (GO:0004518)
Family alignment:
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There are 8355 XPGN domains in 8349 proteins in SMART's nrdb database.

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