The domain within your query sequence starts at position 172 and ends at position 470; the E-value for the Noc2 domain shown below is 1.2e-117.

KEAFLGPILKQMYIMYVRNCKFTSPSTLPLISFMQRTLTEMLALDPSVSYQHAFLYIRQL
AVHLRNAMTAGKKETHQSVYNWQYVHCLYLWCRVLSTLGSSEILQPLLYPLSQIIIGCIK
LLPTARFYPLRMHCVRALTLLSQTIGTFIPVLPFILEIFQQVDFNRRPGRMSSKPINFSV
ILKLSSTNLQEKAYRDGLLEQLCDLTLEYLHSQAHSIAFPELVLPTVLQLKSFLRECKVA
NYCRQVRQLLEKVQENAQHIQSLRQSATFSVSDQMAVDAWEKQVREEGTPLTRYYGHWK

Noc2

Noc2
PFAM accession number:PF03715
Interpro abstract (IPR005343):

In Saccharomyces cerevisiae, Noc2 forms a nucleolar complex with Mak21 that binds to 90S and 66S pre-ribosomes. It also forms a nuclear complex with Noc3 that binds to 66S pre-ribosomes [ (PUBMED:11371346) ]. Both complexes mediate intranuclear transport of ribosomal precursors [ (PUBMED:11371346) ].

In humans, Noc2 (also known as NIR) acts as an inhibitor of histone acetyltransferase activity; prevents acetylation of all core histones by the EP300/p300 histone acetyltransferase at p53/TP53-regulated target promoters in a histone deacetylases (HDAC)-independent manner. It also acts as a transcription corepressor of p53/TP53- and TP63-mediated transactivation of the p21/CDKN1A promoter. It is involved in the regulation of p53/TP53-dependent apoptosis [ (PUBMED:16322561) (PUBMED:20123734) (PUBMED:20959462) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Noc2