NO66_DROYA
ID NO66_DROYA Reviewed; 683 AA.
AC B4Q068;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=GE16340;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000162; EDX01220.1; -; Genomic_DNA.
DR RefSeq; XP_002100112.1; XM_002100076.2.
DR AlphaFoldDB; B4Q068; -.
DR SMR; B4Q068; -.
DR STRING; 7245.FBpp0261350; -.
DR EnsemblMetazoa; FBtr0262858; FBpp0261350; FBgn0233870.
DR GeneID; 6524249; -.
DR KEGG; dya:Dyak_GE16340; -.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_2_1_1; -.
DR OMA; EWGCMAG; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; B4Q068; -.
DR Proteomes; UP000002282; Chromosome X.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblMetazoa.
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; Phosphoprotein; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..683
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390994"
FT DOMAIN 341..480
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 381
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 383
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 446
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 683 AA; 76493 MW; 841872F89FC74CF1 CRC64;
MHKASTSSAN RANFQGNHKT QKSPNNGKAK AKKSPNTDIN VADVEMLLNP RSNLTKEQKE
RRKMMEGFVT KTFERAENES DGSDIDTSAS TSNKGKSKAA RPTDRKRRLQ AEDSPPADAN
NNNTKNGKDG KVSKESASTQ GASATKRKPP RSQGLEHTSP IQVDGEALAC PLVRKSLPAA
GASGASGPAK SCPLPEKRKS LPAGAAKSKS QVIKQEALEE ASNEAQLLAL PIETHKTDSI
EEGRRVLQWL LNPIKVNHFF DDFWEHTAFV VQRKNPHYYS KLISFKMIDE MLVRHRLDFT
INVDVTTYKN GKRETLNPEG RALPPVVWGL YSEGCSIRIL NPSTYLVGLR QVCSIMQEFF
HCLVGANVYL TPPNSQGFAP HYDDIEAFVI QVEGRKRWRL YEPPSGSDQL CRNSSSNFDQ
EQLGEPILDE VLEAGDLLYF PRGTVHQAIT EEEQHSLHIT LSVYQQQAYV NLLEKLMPIV
LKKAIKQSVA LRRGLPLHTF HVLGEAQRAN RSDSRNQLVE NVQKLVTKHL MPSAQDIDEA
VDQLAKKFQH EALPPIILPE EQVRTVFGSR STADEQGNAI CDYEFDTKTS VRLLRANILR
LVTEEDGSVR IYHHVDNGFE YCKYEPIFME ILPEEAAAVE LLISAYPYYL TVGQMPLDSA
ARKVEVVTAL WERGLLMTEK PFK
