CDC48 N-terminal domain
| CDC48_N | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of aaa atpase p97/vcp nd1 in complex with p47 c | |||||||||
| Identifiers | |||||||||
| Symbol | CDC48_N | ||||||||
| Pfam | PF02359 | ||||||||
| InterPro | IPR003338 | ||||||||
| SCOP | 1cz4 | ||||||||
| SUPERFAMILY | 1cz4 | ||||||||
| |||||||||
| CDC48_2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 amino terminal domain of the n-ethylmaleimide sensitive fusion protein (nsf) | |||||||||
| Identifiers | |||||||||
| Symbol | CDC48_2 | ||||||||
| Pfam | PF02933 | ||||||||
| Pfam clan | CL0402 | ||||||||
| InterPro | IPR004201 | ||||||||
| SCOP | 1cz4 | ||||||||
| SUPERFAMILY | 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.
References
- ↑ Coles M, Diercks T, Liermann J, Groger A, Rockel B, Baumeister W, Koretke KK, Lupas A, Peters J, Kessler H (October 1999). "The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple betaalphabetabeta element". Curr. Biol. 9 (20): 1158–68. doi:10.1016/S0960-9822(00)80017-2. PMID 10531028.
This article incorporates text from the public domain Pfam and InterPro IPR003338
This article incorporates text from the public domain Pfam and InterPro IPR004201