Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7 (EC 1.14.11.63) (EC 3.4.-.-) (JmjC domain-containing protein 7) (Jumonji domain-containing protein 7) (L-lysine (3S)-hydroxylase JMJD7)
1_MAEAA 6_ LEAVR 11_ SELRE 16_ FPAAA 21_ RELCV 26_ PLAVP 31_ YLDKP 36_ PTPLH 41_ FYRDW 46_ VCPNR 51_ PCIIR 56_ NALQH 61_ WPALQ 66_ KWSLP 71_ YFRAT 76_ VGSTE 81_ VSVAV 86_ TPDGY 91_ ADAVR 96_ GDRFM 101_ MPAER 106_ RLPLS 111_ FVLDV 116_ LEGRA 121_ QHPGV 126_ LYVQK 131_ QCSNL 136_ PSELP 141_ QLLPD 146_ LESHV 151_ PWASE 156_ ALGKM 161_ PDAVN 166_ FWLGE 171_ AAAVT 176_ SLHKD 181_ HYENL 186_ YCVVS 191_ GEKHF 196_ LFHPP 201_ SDRPF 206_ IPYEL 211_ YTPAT 216_ YQLTE 221_ EGTFK 226_ VVDEE 231_ AMEKV 236_ PWIPL 241_ DPLAP 246_ DLARY 251_ PSYSQ 256_ AQALR 261_ CTVRA 266_ GEMLY 271_ LPALW 276_ FHHVQ 281_ QSQGC 286_ IAVNF 291_ WYDME 296_ YDLKY 301_ SYFQL 306_ LDSLT 311_KASGL
1: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase (PubMed:28847961, PubMed:29915238). 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 (PubMed:28847961). Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4 (PubMed:28847961). After initial cleavage, continues to digest histones tails via its aminopeptidase activity (PubMed:28847961). Additionally, may play a role in protein biosynthesis by modifying the translation machinery (PubMed:29915238). 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) (PubMed:29915238)