The ELM2 (EGL-27 and MTA1 homology) domain was first described in Egl-27, a Caenorhabditis elegans protein that plays a fundamental role in patterning during embryonic development [1]. Most ELM2 domain-containing proteins also possess a SANT domain, implying a structural and/or functional relationship between these two motifs. Many proteins containing an ELM2 domain are known components of characterized transcription- and chromatin-regulatory complexes containing one or more histone deacetylases (HDACs). The evolutionarily conserved ELM2 domain has been shown to function as a transcriptional repression domain through recruitment of HDAC activity [2].

Some proteins known to contain a ELM2 domain are listed below:

• Vertebrate mesoderm induction early response 1 (MI-ER1), a nuclear protein that contains an N-terminal acidic domain with potent transcriptional activity.
• Vertebrate CoREST, a developmental regulator.
• Mammalian metastasis-associated protein MTA1, a component of the NURD complex, which has histone deacetylase and ATP-dependent nucleosome remodelling activities.
• Mammalian metastasis-associated protein MTA2, a component of a chromatin regulatory complex.
• Mammalian metastasis-associated protein MTA3.
• Drosophila melanogaster MTA1-like.
• Drosophila melanogaster GRUNGE (Gug).
• Drosophila melanogaster transcriptional corepressor Atro.
• Caenorhabditis elegans Egl-27 and Egr-1. They are redundantly required for embryonic patterning.

The profile we developed covers the entire extended ELM2 domain [2].