Homologous Superfamily

Ubiquitin activating enzyme, alpha domain superfamily (IPR023318)

Short name: Ub_act_enz_dom_a_sf

Overlapping entries


Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2) [PMID: 1986373]. This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP [PMID: 11004499]. Not all proteins in this entry contain a functional active site.

This superfamily represents an alpha orthogonal bundle domain found in ubiquitin-activating enzyme and ubiquitin-like NEDD8-activating enzyme.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016881 acid-amino acid ligase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.