The domain within your query sequence starts at position 97 and ends at position 167; the E-value for the ZnF_UBR1 domain shown below is 1.24e-35.



Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway
SMART accession number:SM00396
Description: Domain is involved in recognition of N-end rule substrates in yeast Ubr1p
Interpro abstract (IPR003126):

It has been observed that the identity of N-terminal residues of a protein is related to the half life of the protein. This observation yields a rule, called the N-end rule [ (PUBMED:8901547) ]. Similar but distinct versions of the N-end rule operate in all organisms examined, from mammals to fungi and bacteria. In eukaryotes, the N-end rule pathway is a part of the ubiquitin degradation system. Some proteins that have a very short half life contain a specific motif at their N terminus, the N-degron. It consists of a destabilising N-terminal residue and an internal Lys, which is the site of poly-Ub chain [ (PUBMED:8901547) (PUBMED:10545113) ].

The UBR1 protein was shown to bind specifically to proteins bearing N-terminal residues that are destabilising according to the N-end rule, but not to otherwise identical proteins bearing stabilising N-terminal residues [ (PUBMED:10581257) ]. UBR1 contains an N-terminal conserved region (the UBR-type zinc finger) which is also found in various proteins implicated in N-degron recognition. The UBR-type zinc finger defines a unique E3 class, most likely N-degron specific [ (PUBMED:16055722) ].

GO function:zinc ion binding (GO:0008270)
Family alignment:
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There are 2060 ZnF_UBR1 domains in 2051 proteins in SMART's nrdb database.

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