NO66_DROPE
ID NO66_DROPE Reviewed; 687 AA.
AC B4GUZ2;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=GL12933;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479192; EDW26529.1; -; Genomic_DNA.
DR RefSeq; XP_002022494.1; XM_002022458.1.
DR AlphaFoldDB; B4GUZ2; -.
DR SMR; B4GUZ2; -.
DR STRING; 7234.FBpp0177040; -.
DR PRIDE; B4GUZ2; -.
DR EnsemblMetazoa; FBtr0178548; FBpp0177040; FBgn0150539.
DR GeneID; 6597402; -.
DR KEGG; dpe:6597402; -.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_2_1_1; -.
DR OMA; IRFQHEA; -.
DR PhylomeDB; B4GUZ2; -.
DR Proteomes; UP000008744; 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..687
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390988"
FT DOMAIN 347..483
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 387
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 389
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 449
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 687 AA; 76299 MW; 3BF47CECBCA276C8 CRC64;
MSDKNKKVSA FAAYRGSATS KNDVQKGTKN SDKNGAAKNN NNRNLASKNG GKQKGPPKKN
GSYSDGDNGS SSSSGEDEED DSTDSSDEYE SSESGEEYTL NSHSSQSSPE TPANTRESLK
RRNDEAEGSN PIGAKRTSST PVGQSTSAAR STQQPKAPSC PLQRRSCPLP SKKNTVPVKV
EVASPDRALL SPQSIKKEPG ASMLCRIKIG LVKSVQPGGD AGAEAGAGQA VNRLEPCHKV
HKENSIEVGK RTLAQLIAPM TMATFLRDHW EKSPFRVKTT TSGGFSNLIS FKMIDQMLIQ
NHVEYTTNID VTSYEDGVRK TLNPDGRALP PSVWAHYQRG CSIRILNPSS YLVQLRQLCV
KLQEFFHCLV GANVYLTPPE SQGFAPHYDD IEAFVLQVEG KKRWRIYAPT KELPRESSGN
LSQTELGDPI MDIVLKPGDL LYFPRGWIHQ AITEKDSHSL HITLSAYQQQ SYANLMEKLM
PLVVKESVEQ TLKLRKGLPL DIFQNLGVAN AEWKGAHRQK LIQHIQNLAQ RLVPTEGQID
RALDQLAIKF QHEALPPTIA PQELKRTVFG AQATADRNGH CSLDYELAEG TAVRLLRANI
VRLTVDEGVL RCYYYTDNGL EYCKYEPNFF ELEPFHGTVI ETLIHAYPEY TKIKDLPPMG
NDEDRLEFVE ALWERGILMV EKPFKKL
