|PROSITE documentation PDOC50164 [for PROSITE entry PS50164]|
Nucleases of the GIY-YIG family are involved in many cellular processes, including DNA repair and recombination, transfer of mobile genetic elements, and restriction of incoming foreign DNA. The GIY-YIG superfamily groups together nucleases characterized by the presence of a domain of typically ~100 amino acids, with two short motifs "GIY" and "YIG" in the N-terminal part, followed by an Arg residue in the center and a Glu residue in the C-terminal part [1,2,3,4,5].
The GIY-YIG domain forms a compact structural domain, which serves as a scaffold for the coordination of a divalent metal ion required for catalysis of the phosphodiester bond cleavage. The GIY-YIG domain has an α/β-sandwich architecture with a central three-stranded antiparallel β-sheet flanked by three-helices (see <PDB:1MK0>). The three-stranded anti-parallel β-sheet contains the GIY-YIG sequence elements. The most conserved and putative catalytic residues are located on a shallow, concave surface and include a metal coordination site [2,3,4,5].
Some proteins known to contain a GIY-YIG domain are listed below:
The profile we developed covers the entire GIY-YIG domain.Last update:
May 2012 / Profile and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Kowalski J.C., Belfort M., Stapleton M.A., Holpert M., Dansereau J.T., Pietrokovski S., Baxter S.M., Derbyshire V.|
|Title||Configuration of the catalytic GIY-YIG domain of intron endonuclease I-TevI: coincidence of computational and molecular findings.|
|Source||Nucleic Acids Res. 27:2115-2125(1999).|
|2||Authors||Van Roey P., Meehan L., Kowalski J.C., Belfort M., Derbyshire V.|
|Title||Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI.|
|Source||Nat. Struct. Biol. 9:806-811(2002).|
|3||Authors||Truglio J.J., Rhau B., Croteau D.L., Wang L., Skorvaga M., Karakas E., DellaVecchia M.J., Wang H., Van Houten B., Kisker C.|
|Title||Structural insights into the first incision reaction during nucleotide excision repair.|
|Source||EMBO J. 24:885-894(2005).|
|4||Authors||Dunin-Horkawicz S., Feder M., Bujnicki J.M.|
|Title||Phylogenomic analysis of the GIY-YIG nuclease superfamily.|
|Source||BMC Genomics 7:98-98(2006).|
|5||Authors||Ibryashkina E.M., Sasnauskas G., Solonin A.S., Zakharova M.V., Siksnys V.|
|Title||Oligomeric structure diversity within the GIY-YIG nuclease family.|
|Source||J. Mol. Biol. 387:10-16(2009).|