CDC48 N-terminal domain

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.

CDC48_N
crystal structure of aaa atpase p97/vcp nd1 in complex with p47 c
Identifiers
Symbol	CDC48_N
Pfam	PF02359
InterPro	IPR003338
SCOP2	1cz4 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

CDC48_2
amino terminal domain of the n-ethylmaleimide sensitive fusion protein (nsf)
Identifiers
Symbol	CDC48_2
Pfam	PF02933
Pfam clan	CL0402
InterPro	IPR004201
SCOP2	1cz4 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary