NO66_DROMO
ID NO66_DROMO Reviewed; 888 AA.
AC B4L6Q5;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66;
DE EC=1.14.11.-;
DE EC=1.14.11.27;
DE AltName: Full=Histone lysine demethylase NO66;
GN ORFNames=GI16410;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Oxygenase that can act as both a histone lysine demethylase
CC and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-
CC 4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a
CC central role in histone code (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.27;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ROX family. NO66 subfamily. {ECO:0000305}.
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DR EMBL; CH933812; EDW06051.1; -; Genomic_DNA.
DR RefSeq; XP_002011209.2; XM_002011173.2.
DR AlphaFoldDB; B4L6Q5; -.
DR SMR; B4L6Q5; -.
DR STRING; 7230.FBpp0165627; -.
DR GeneID; 6585581; -.
DR KEGG; dmo:Dmoj_GI16410; -.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_2_0_1; -.
DR InParanoid; B4L6Q5; -.
DR OMA; WERNACQ; -.
DR Proteomes; UP000009192; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; ISS:UniProtKB.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0070544; P:histone H3-K36 demethylation; ISS:UniProtKB.
DR GO; GO:0034720; P:histone H3-K4 demethylation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR039994; JmjC_protein.
DR PANTHER; PTHR13096; PTHR13096; 1.
DR Pfam; PF08007; Cupin_4; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..888
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390987"
FT DOMAIN 564..709
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 83..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..333
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 610
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 612
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 675
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 888 AA; 99001 MW; E309084C4ABCCDF5 CRC64;
MDRISAYAAY GLAPKKTSKR STMKIAKHFS KKNAKKTKEA MAAKKEARKA AAKAALREVR
KLERKAAADK AAKIAADKAA DKAAAKAAAK AAKKAAKREK NIAKKQPEKS AAGVTENVQK
QLENGQENNG TLINLSNGKQ HQKPKAAKMS SSNGSFSGID SDFLNSSDFG STEDSFMSGS
GDSFDYSNNS DFDFDSDGDS NDFDDSDAAA SSCASCEYFD MDSNMVVGQE SDTNGNSYMH
NGTTQSEDQF TEEYTLSSIF NSTSSSGANP IKVEPRKAAK RNEPFDLNNN KNKPTAAKQP
KMSLKQEQAQ VGKQRADPAP SCPLPPRPSK TMIKSCPLPP KAPAAKPVPN KCRLSSRESL
TKTGAKSCRL SSAPADKMAN KMAAPSRKSS SKNKNNDNNN IDTNNKKDAN NKKDANNNKD
INNKKDANNN KDTNNNKDNN NKNKLSSNVS QLVTGNEKQR GPVHLENSIE EGKRMLNWLL
NPITSETFFE QYWERNACQV KRKQPNYFTQ LISFQMIDEM LIENQLEFTT NIDVTTYKKG
VRQTLNPVGR AMSPAIWGYY GDGCSIRILN PSTYLPKLRQ LCSTMQEFFH CLVGANVYLT
PPNSQGFAPH YDDIEAFVIQ VEGRKRWRLY APPHQSDVLA RTSSGNYKQE ELGQPLFDAV
LEAGDILYFP RGTVHQAVTE PKQHSLHITL SVYQQQAYAN LLEVLMPSVL ERAIKHHLSL
RRGLPLHIWQ HVGLAKGGQQ SEQRDQLMNS TKQLVQRYLV PTEAQIDAAV DQLAKRFQHE
ALPPYIKPEE SMRTTKVRLL RRQHPAPGGR RQQLRVYYYV DNALEYCKNE PNYMEIQPTE
APAVEALMTT YPAYLKVGKL PLRSADRRIE VATALWERGL LMTEKPFK
