The domain within your query sequence starts at position 10 and ends at position 79; the E-value for the ubiquitin domain shown below is 3.1e-9.



PFAM accession number:PF00240
Interpro abstract (IPR000626):

Ubiquitin is a protein of 76 amino acid residues, found in all eukaryotic cells and whose sequence is extremely well conserved from protozoan to vertebrates. Ubiquitin acts through its post-translational attachment (ubiquitinylation) to other proteins, where these modifications alter the function, location or trafficking of the protein, or targets it for destruction by the 26S proteasome [(PUBMED:15454246)].

Ubiquitin is a globular protein, the last four C-terminal residues (Leu-Arg-Gly-Gly) extending from the compact structure to form a 'tail', important for its function. The latter is mediated by the covalent conjugation of ubiquitin to target proteins, by an isopeptide linkage between the C-terminal glycine and the epsilon amino group of lysine residues in the target proteins.

Ubiquitin is expressed as three different precursors: a polymeric head-to-tail concatemer of identical units (polyubiquitin), and two N-terminal ubiquitin moieties, UbL40 and UbS27, that are fused to the ribosomal polypeptides L40 and S27, respectively. Specific endopeptidases cleave these precursor molecules [(PUBMED:15571815)] to release ubiquitin moieties that are identical in sequence and contribute to the ubiquitin pool [(PUBMED:16185873)]. Some organisms express additional ubiquitin fusion proteins [(PUBMED:12729753)]. Furthermore, there are several ubiquitin-like proteins derived from ubiquitin [(PUBMED:12826404)].

This entry represents a domain characteristic of ubiquitin (Ub) and ubiquitin-like (Ubl) proteins such as SUMO [(PUBMED:17491593), (PUBMED:15479240)] and Nedd8 [(PUBMED:9857030)].

GO function:protein binding (GO:0005515)

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