Nascent polypeptide-associated complex NAC domain (IPR002715)

Short name: Nas_poly-pep-assoc_cplx_dom

Overlapping homologous superfamilies

Domain relationships



In eukaryotes, the Nascent polypeptide-Associated Complex (NAC) is a heterodimeric cytosolic protein complex composed of NAC alpha and NAC beta. 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 [PMID: 12475173]. Alpha and beta NACs share homology with each other, both contain a NAC A/B domain. In archaea no beta NAC proteins are found; the complex is an homodimer of NAC alpha [PMID: 10413400, PMID: 15665334].

The crystal structure of an archeal NAC has been solved [PMID: 15665334]. The NAC A/B domain consists of six strands arranged in a beta 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.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles