| Symbol: | CDC48_N |
| CDC48_N | |
| Pfam: | PF02359 |
| Interpro: | IPR003338 |
| Scop: | 1cz4 |
| Symbol: | CDC48_2 |
| CDC48_2 | |
| Pfam: | PF02933 |
| Pfam Clan: | CL0402 |
| Interpro: | IPR004201 |
| Scop: | 1cz4 |
In molecular biology, the CDC48 N-terminal domain is a protein domain found in AAA ATPases including cell division protein 48 (CDC48), VCP-like ATPase and N-ethylmaleimide sensitive fusion protein. It is a substrate recognition domain which binds polypeptides, prevents protein aggregation, and catalyses refolding of permissive substrates. It is composed of two equally sized subdomains. The amino-terminal subdomain (CDC48_N) forms a double-psi beta-barrel whose pseudo-twofold symmetry is mirrored by an internal sequence repeat of 42 residues. The carboxy-terminal subdomain (CDC48_2) forms a novel six-stranded beta-clam fold.[1] Together these subdomains form a kidney-shaped structure, in close agreement with results from electron microscopy. CDC48_N is related to numerous proteins including prokaryotic transcription factors, metabolic enzymes, the protease cofactors UFD1 and PrlF, and aspartic proteinases.