ATG7 was identified based on homology to Pichia pastoris GSA7 and Saccharomyces cerevisiae APG7. In the yeast, the protein appears to be required for fusion of peroxisomal and vaculuolar membranes. The protein shows homology to the ATP-binding and catalytic sites of the E1 ubiquitin activating enzymes.
The deduced 703-amino acid protein contains a central putative E1-like ATP-binding site (GxGxxG), conserved charged amino acids flanking the GxGxxG motif, and a putative E1 active site with a conserved catalytic cysteine. APG7L shares similarity with the E1 enzymes UBA2 and UBA3 (UBE1C), and it shares 38% identity with yeast Apg7. EST database analysis indicated that APG7L is expressed by many diverse tissues.