| Description | Proteins in this entry are part of the wider so-called "phage"integrase fmaily which describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci.This entry represents the chromosomally-encoded polypeptide XerD, which is closely related to, and interacts with, another chromosomally-encoded polypeptide, XerC ( ). These proteins are site-specific tyrosine recombinases, which act by catalyzing the cutting and rejoining of the recombining DNA molecules [ ]. They form a cyclic heterotetrameric complex composed of two molecules of XerC and two molecules of XerD. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.XerD is composed of two domains, an N-terminal α-helical domain, and a C-terminal domain composed mostly of α helices, with a three-stranded antiprallel β sheet along one edge [ ]. The active site is found at the extreme C-terminal end of the polypeptide. Most of the C-terminal domain is structurally homologous to that of other "phage"integrases, but the active site regions of these enzymes are stucturally distinct. | Name | Tyrosine recombinase XerD |
| Short Name | Recomb_XerD | Type | Family |
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