SMART: Pfam domain EAF

The domain within your query sequence starts at position 14 and ends at position 114; the E-value for the EAF domain shown below is 3.4e-26.

HCLRLGESFEKRPRASFHTIRYDFKPASIDTSCEGELQVGKGDEVTITLPHIPGSTPPMT
VFKGNKRPYQKDCVLIINHDTGEYVLEKLSSSIQVKKTRAE

EAF

PFAM accession number:	PF09816
Interpro abstract (IPR019194):	This entry represents the N-terminal domain of ELL-associated factor (Eaf) proteins, which act as transcriptional transactivators of ELL and ELL2 RNA Polymerase II (Pol II) transcriptional elongation factors [ (PUBMED:11418481) (PUBMED:12686606) (PUBMED:16006523) (PUBMED:16006523) ]. Eaf proteins form a stable heterodimer complex with ELL proteins to facilitate the binding of RNA polymerase II to activate transcription elongation. ELL and EAF1 are components of Cajal bodies, which have a role in leukemogenesis [ (PUBMED:12686606) ]. EAF1 also has the capacity to interact with ELL1 and ELL2. The N terminus of approx 120 of EAF1 has a region of high serine, aspartic acid, and glutamic acid residues [ (PUBMED:11418481) (PUBMED:17150956) ].

PFAM accession number:

PF09816

Interpro abstract (IPR019194):

This entry represents the N-terminal domain of ELL-associated factor (Eaf) proteins, which act as transcriptional transactivators of ELL and ELL2 RNA Polymerase II (Pol II) transcriptional elongation factors [ (PUBMED:11418481) (PUBMED:12686606) (PUBMED:16006523) (PUBMED:16006523) ]. Eaf proteins form a stable heterodimer complex with ELL proteins to facilitate the binding of RNA polymerase II to activate transcription elongation. ELL and EAF1 are components of Cajal bodies, which have a role in leukemogenesis [ (PUBMED:12686606) ]. EAF1 also has the capacity to interact with ELL1 and ELL2. The N terminus of approx 120 of EAF1 has a region of high serine, aspartic acid, and glutamic acid residues [ (PUBMED:11418481) (PUBMED:17150956) ].

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