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.

QLCGKVFKSGETTYSCRDCAIDPTCVLCMDCFQSSVHKNHRYKMHTSTGGGFCDCGDTEA
WKTGPFCVDHE

ZnF_UBR1

Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway
ZnF_UBR1
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:
View or

There are 2060 ZnF_UBR1 domains in 2051 proteins in SMART's nrdb database.

Click on the following links for more information.