Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase (, ). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation . Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4 . After initial cleavage, continues to digest histones tails via its aminopeptidase activity . Additionally, may play a role in protein biosynthesis by modifying the translation machinery . Acts as a Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys-21' of DRG2 translation factors (TRAFAC), promoting their interaction with ribonucleic acids (RNA) .
Subcellular locations: Nucleus, Cytoplasm