PROSITE documentation PDOC51151
NAC A/B domain profile


In eukaryote, the Nascent polypeptide-Associated Complex (NAC) is a heterodimeric cytosolic protein complex composed of NAC α and NAC β. NAC binds reversibly to the ribosome where it is in contact with nascent chains as they emerge from the ribosome. But the cellular function of NAC seems to be much more diverse as it is also involved in transcription regulation and mitochondrial translocation [1]. α and β NACs share homology with each other, both contain a NAC A/B domain. In archaea no β NAC proteins are found; the complex is an homodimer of NAC α [2,3].

The crystal structure of an archeal NAC has been solved (see <PDB:1TR8>) [3]. The NAC A/B domain consists of six strands arranged in a β barrel structure similar to the OB fold. Various OB folds interact with ribosomal RNA which could suggest a similar role for the NAC A/B domain.

The profile we developed covers the whole NAC A/B domain.

Last update:

October 2005 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

NAC_AB, PS51151; NAC A/B domain profile  (MATRIX)


1AuthorsRospert S. Dubaquie Y. Gautschi M.
TitleNascent-polypeptide-associated complex.
SourceCell. Mol. Life Sci. 59:1632-1639(2002).
PubMed ID12475173

2AuthorsMakarova K.S. Aravind L. Galperin M.Y. Grishin N.V. Tatusov R.L. Wolf Y.I. Koonin E.V.
TitleComparative genomics of the Archaea (Euryarchaeota): evolution of conserved protein families, the stable core, and the variable shell.
SourceGenome Res. 9:608-628(1999).
PubMed ID10413400

3AuthorsSpreter T. Pech M. Beatrix B.
TitleThe crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain.
SourceJ. Biol. Chem. 280:15849-15854(2005).
PubMed ID15665334

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