{PDOC51151}
{PS51151; NAC_AB}
{BEGIN}
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* NAC A/B domain profile *
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In   eukaryote,   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  [1].  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 [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 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.

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

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2005 / First entry.

[ 1] Rospert S., Dubaquie Y., Gautschi M.
     "Nascent-polypeptide-associated complex."
     Cell. Mol. Life Sci. 59:1632-1639(2002).
     PubMed=12475173
[ 2] Makarova K.S., Aravind L., Galperin M.Y., Grishin N.V., Tatusov R.L.,
     Wolf Y.I., Koonin E.V.
     "Comparative genomics of the Archaea (Euryarchaeota): evolution of
     conserved protein families, the stable core, and the variable shell."
     Genome Res. 9:608-628(1999).
     PubMed=10413400
[ 3] Spreter T., Pech M., Beatrix B.
     "The crystal structure of archaeal nascent polypeptide-associated
     complex (NAC) reveals a unique fold and the presence of a
     ubiquitin-associated domain."
     J. Biol. Chem. 280:15849-15854(2005).
     PubMed=15665334; DOI=10.1074/jbc.M500160200

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