SMART: Pfam domain NAC

The domain within your query sequence starts at position 1357 and ends at position 1413; the E-value for the NAC domain shown below is 2.9e-24.

EKKARKAMSKLGLRQIQGVTRITIQKSKNILFVIAKPDVFKSPASDTYVVFGEAKIE

NAC

PFAM accession number:	PF01849
Interpro abstract (IPR002715):	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 [ (PUBMED: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 [ (PUBMED:10413400) (PUBMED:15665334) ]. The crystal structure of an archeal NAC has been solved [ (PUBMED: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.

PFAM accession number:

PF01849

Interpro abstract (IPR002715):

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 [ (PUBMED: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 [ (PUBMED:10413400) (PUBMED:15665334) ].

The crystal structure of an archeal NAC has been solved [ (PUBMED: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.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry NAC