Cell division protein 48 (CDC48) N-terminal domain
SMART accession number:
SM01073
Description:
This domain has a double psi-beta barrel fold and includes VCP-like ATPase and N-ethylmaleimide sensitive fusion protein N-terminal domains. Both the VAT and NSF N-terminal functional domains consist of two structural domains of which this is at the N-terminus. The VAT-N domain found in AAA ATPases is a substrate 185-residue recognition domain (PUBMED:10531028).
This entry represents the amino-terminal subdomain.
The CDC48 N-terminal domain is a protein domain found in AAA ATPases including cell division protein 48 (CDC48), VCP-like ATPase (VAT) 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 forms a double-psi beta-barrel whose pseudo-twofold symmetry is mirrored by an internal sequence repeat of 42 residues. The carboxy-terminal subdomain forms a novel six-stranded beta-clam fold [ (PUBMED:10531028) ]. Together these subdomains form a kidney-shaped structure.
Family alignment:
There are 6871 CDC48_N domains in 6866 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing CDC48_N domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with CDC48_N domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing CDC48_N domain in the selected taxonomic class.
The solution structure of VAT-N reveals a 'missing link' in the evolutionof complex enzymes from a simple betaalphabetabeta element.
Curr Biol. 1999; 9: 1158-68
Display abstract
BACKGROUND: The VAT protein of the archaebacterium Thermoplasmaacidophilum, like all other members of the Cdc48/p97 family of AAAATPases, has two ATPase domains and a 185-residue amino-terminalsubstrate-recognition domain, VAT-N. VAT shows activity in protein foldingand unfolding and thus shares the common function of these ATPases indisassembly and/or degradation of protein complexes. RESULTS: Usingnuclear magnetic resonance (NMR) spectroscopy, we found that VAT-N iscomposed of two equally sized subdomains. The amino-terminal subdomainVAT-Nn (comprising residues Met1-Thr92) forms a double-psi beta-barrelwhose pseudo-twofold symmetry is mirrored by an internal sequence repeatof 42 residues. The carboxy-terminal subdomain VAT-Nc (comprising residuesGlu93-Gly185) forms a novel six-stranded beta-clam fold. Together, VAT-Nnand VAT-Nc form a kidney-shaped structure, in close agreement with resultsfrom electron microscopy. Sequence and structure analyses showed thatVAT-Nn is related to numerous proteins including prokaryotic transcriptionfactors, metabolic enzymes, the protease cofactors UFD1 and PrlF, andaspartic proteinases. These proteins map out an evolutionary path fromsimple homodimeric transcription factors containing a single copy of theVAT-Nn repeat to complex enzymes containing four copies. CONCLUSIONS: Ourresults suggest that VAT-N is a precursor of the aspartic proteinases thathas acquired peptide-binding activity while remaining proteolyticallyincompetent. We propose that the binding site of the protein is similar tothat of aspartic proteinases, in that it lies between the psi-loops of theamino-terminal beta-barrel and that it coincides with a crescent-shapedband of positive charge extending across the upper face of the molecule.
Crystal Structure of FAF1 UBX Domain In Complex with p97/VCP N Domain Reveals The Conserved FcisP Touch-Turn Motif of UBX Domain Suffering Conformational Change
