Biology:YDG SRA protein domain

From HandWiki
YDG Set and Ring Associated protein domain
Identifiers
SymbolYDG_SRA
PfamPF02182
InterProIPR003105
SMARTSRA

In molecular biology, this protein domain has been termed SRA-YDG, which is the abbreviation for SET and Ring finger Associated, YDG motif. Additional characteristics of the domain include conservation of up to 13 evenly spaced glycine residues and a VRV(I/V)RG motif. The protein domain is mainly found in plants and animals and in bacteria.

Function

The function of this protein domain, in animals, is to aid progression through the cell cycle. This domain is associated with the Np95-like ring finger protein and the related gene product Np97, which contains PHD and RING FINGER domains; important in cell cycle progression. Np95 is a chromatin-associated ubiquitin ligase, binding to histones is direct and shows a remarkable preference for histone H3 and its N-terminal tail. The SRA-YDG domain contained in Np95 is needed for the interaction with histones and for chromatin binding in vivo.[1][2]

In plants the SRA-YDG domain is associated with the SET domain, found in a family of histone methyl transferases, which switch genes "off" by adding a methyl group. In bacteria it is found in association with HNH, a non-specific nuclease motif.[2][3]

Structure

This protein domain contains both alpha helices and beta sheets. In particular, the beta sheets are arranged in an antiparallel formation. More specifically, it contains a beta grasp fold.

References

  1. "Cloning and mapping of Np95 gene which encodes a novel nuclear protein associated with cell proliferation". Mamm. Genome 9 (12): 1032–5. December 1998. doi:10.1007/s003359900920. PMID 9880673. 
  2. 2.0 2.1 "Np95 is a histone-binding protein endowed with ubiquitin ligase activity". Mol. Cell. Biol. 24 (6): 2526–35. March 2004. doi:10.1128/MCB.24.6.2526-2535.2004. PMID 14993289. 
  3. "The Arabidopsis thaliana genome contains at least 29 active genes encoding SET domain proteins that can be assigned to four evolutionarily conserved classes". Nucleic Acids Res. 29 (21): 4319–33. November 2001. doi:10.1093/nar/29.21.4319. PMID 11691919. 
This article incorporates text from the public domain Pfam and InterPro: IPR003105