NO66_DROSI
ID NO66_DROSI Reviewed; 847 AA.
AC B4R4H1;
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=GD16684;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; CM000366; EDX17061.1; -; Genomic_DNA.
DR AlphaFoldDB; B4R4H1; -.
DR SMR; B4R4H1; -.
DR STRING; 7240.B4R4H1; -.
DR PRIDE; B4R4H1; -.
DR HOGENOM; CLU_013645_2_1_1; -.
DR PhylomeDB; B4R4H1; -.
DR Proteomes; UP000000304; Chromosome x.
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; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..847
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390991"
FT DOMAIN 499..644
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 545
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 547
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
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 MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 847 AA; 94924 MW; 8EF969F0EF4982B1 CRC64;
MEKVTNSAAA KPQGNNKKQE SAYNGTAKDK KKPNLDIETT DSDLLSDIHL DGTKEQKVQT
LFSKVFEDTG PSTAKTADRK RRLQAEADAN NNDTEKASKL AKTSVATTDM DLRVTRKQHT
FYMKVQALLA EHAEKESTKK ASKMAKISEA DLILFMTQKE IEYYMKVKAL IAKCAEEGSK
LLDNWTSSKD IAKTADHERR LQAEADAKNN DTKKAGQSAK ESVATTDMQL NVIKEQMEHC
KKVQALLANE SKGAEKESKV LDYSTGPSTS SKEAAAAKTA DHERRLLAEA DVNNNDTEKA
GQSAMESVAT QGASATERKQ SFSLGLEHTS PIQVNGAALA CPLVRKSLPP GEANSCPPPP
KRDPAAVKSS VKIIKVKAPE EGNNNNDEKE MSTETSETHK TDSVEEGRRV VKWIIFPIKP
NFFFKYFWEQ TACLVQRTNP KYFQSLISFK MLDEILIRHH LDFTVNLDVT TYKNGKRETL
NPEGRALPPA VWGFYSEGCS IRLLNPSAYL TRLREVCTVL QEFFHCKVEA NMYLTPPNSQ
GFAPHYDDIE AFVIQVEGRK RWLLYEPPKE ADHLARISSG NYDQEQLGKP IIDEVLSAGD
VLYFPRGTVH QAITEEQQHS LHITLSVYQQ QAYANLLETL MPMVLKKAVD RSVALRRGLP
LHTFQVLGNA YKANDCGSRQ LLVENVQKLV TKYLIPSEDD IDEAVDQMAK KFQHEALPPI
VLPSEEVRTV HGARSGADEQ GNCVCDYKFN EKTSVRLLRA NILRLVTEPD GSVRIYHHAD
NGLDYCKYEP YFMEILPEEA KAVELLISAY PYYLTIDQLP LKSSARKVEV ATALWEHGLL
MTEKPFK
