The domain within your query sequence starts at position 29 and ends at position 111; the E-value for the Proteasom_Rpn13 domain shown below is 3.5e-35.

GKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGTVEDDLIIFPDDCEFKRVPQC
PSGRVYVLKFKAGSKRLFFWMQE

Proteasom_Rpn13

Proteasom_Rpn13
PFAM accession number:PF04683
Interpro abstract (IPR006773):

This entry includes Rpn13 from budding yeasts and its homologue, ADRM1 from animals.

Rpn13 is a subunit and an ubiquitin receptor of the 19S regulatory particle of the 26S proteasome lid. The 26S proteasome is a huge macromolecular protein-degradation machine consisting of a proteolytically active 20S core, in the form of four disc-like proteins, and one or two 19S regulatory particles. The regulatory particle(s) sit on the top and or bottom of the core, de-ubiquitinate the substrate peptides, unfold them and guide them into the narrow channel through the centre of the core. Rpn13 and its homologues dock onto the regulatory particle through the N-terminal region which binds Rpn2. The C-terminal part of the domain binds de-ubiquitinating enzyme Uch37/UCHL5 and enhances its isopeptidase activity. Rpn13 binds ubiquitin via a conserved amino-terminal region called the pleckstrin-like receptor for ubiquitin, termed Pru, domain [(PUBMED:18497817)]. The domain forms two contiguous anti-parallel beta-sheets with a configuration similar to the pleckstrin-homology domain (PHD) fold [(PUBMED:18497827)]. Rpn13's ability to bind ubiquitin and the proteasome subunit Rpn2/S1 simultaneously supports evidence of its role as a ubiquitin receptor. Finally, when complexed to di-ubiquitin, via the Pru, and Uch37 via the C-terminal part, it frees up the distal ubiquitin for de-ubiquitination by the Uch37 [(PUBMED:18497827)].

GO component:cytoplasm (GO:0005737), nucleus (GO:0005634)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Proteasom_Rpn13