CDC48 N-terminal domain

{{Short description|Protein domain}}

{{Infobox protein family

| Symbol = CDC48_N

| Name = CDC48_N

| image = PDB 1s3s EBI.jpg

| width =

| caption = crystal structure of aaa atpase p97/vcp nd1 in complex with p47 c

| Pfam = PF02359

| Pfam_clan =

| InterPro = IPR003338

| SMART =

| PROSITE =

| MEROPS =

| SCOP = 1cz4

| TCDB =

| OPM family =

| OPM protein =

| CAZy =

| CDD =

}}

{{Infobox protein family

| Symbol = CDC48_2

| Name = CDC48_2

| image = PDB 1qdn EBI.jpg

| width =

| caption = amino terminal domain of the n-ethylmaleimide sensitive fusion protein (nsf)

| Pfam = PF02933

| Pfam_clan = CL0402

| InterPro = IPR004201

| SMART =

| PROSITE =

| MEROPS =

| SCOP = 1cz4

| TCDB =

| OPM family =

| OPM protein =

| CAZy =

| CDD =

}}

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.{{cite journal |vauthors=Coles M, Diercks T, Liermann J, Groger A, Rockel B, Baumeister W, Koretke KK, Lupas A, Peters J, Kessler H | title = The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple betaalphabetabeta element | journal = Curr. Biol. | volume = 9 | issue = 20 | pages = 1158–68 |date=October 1999 | pmid = 10531028 | doi = 10.1016/S0960-9822(00)80017-2 | s2cid = 6561497 | doi-access = free }} 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.