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This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines.
The G-patch domain is an approximately 48 amino acid domain, which is found in a single copy in several RNA-associated proteins and in type D retroviral polyproteins. It is widespread among eukaryotes but is absent in archaea and bacteria. The G-patch domain has been called after its most notable feature, the presence of six highly conserved glycine residues. The position following the first conserved glycine is occupied almost invariably by an aromatic residue, and several other positions are occupied predominantly by either hydrophobic or small residues. Several groups of G-patch containing proteins are conserved in animals, plants and fungi. In some of these proteins the G- patch is the only recognisable domain but in most of them it is combined with other domains, which include well-defined RNA-binding domains, such as the RRM, dsRBD, SURP and R3H. It has been suggested that the G-patch domain has a specific function in RNA processing and, in particular, that it might be a previously undetected RNA-binding domain mediating a distinct type of RNA-protein interaction.
Aravind L, Koonin EV; , Trends Biochem Sci 1999;24:342-344.: G-patch: a new conserved domain in eukaryotic RNA-processing proteins and type D retroviral polyproteins. PUBMED:10470032 EPMC:10470032.