NO66_DROSE
ID NO66_DROSE Reviewed; 655 AA.
AC B4I100;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=GM12339;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480819; EDW53181.1; -; Genomic_DNA.
DR RefSeq; XP_002037022.1; XM_002036986.1.
DR AlphaFoldDB; B4I100; -.
DR SMR; B4I100; -.
DR STRING; 7238.B4I100; -.
DR EnsemblMetazoa; FBtr0195324; FBpp0193816; FBgn0167276.
DR HOGENOM; CLU_013645_2_1_1; -.
DR OMA; EWGCMAG; -.
DR PhylomeDB; B4I100; -.
DR Proteomes; UP000001292; Unassembled WGS sequence.
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; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..655
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390990"
FT DOMAIN 307..452
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..210
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..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 353
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 355
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 418
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 655 AA; 73306 MW; C91F0855E901E42A CRC64;
MEKVTNSAAA KPQGNNKKQE SAYNGAGKDK KKPNLDIETT DSDLLSDMHL DGTTEQKVGT
LFSKVFEDTD YGTGPSTSSK EAAAAKTADH ERRLQAEADV NNNDAEKAGQ LAKESVATQG
ASATERKQAF SLGLEHTSPI QVNGAALACP LVRKSLPPGE ANSCPPPPKR DPAAVKSAVK
IIKVKAPEEG NNNNDEKEMS TETSEPHKTD SVEEGRRVVM WIIFPIKTKF FFKYFWEQTA
CLVQRTNPKY FQSLISFKML DEILIRHNLD FTVNLDVTTY KNGKRETLNP EGRALPPAVW
GFYSEGCSIR LLHASAYLTR LREVCTVLQE FFHCKVGANM YLTPPNSQGF APHYDDIEAF
VIQVEGRKRW LLYDPPKEAD HLARISSGNY NQEQLGKPII DEVLSAGDVL YFPRGTVHQA
ITEEQQHSLH ITLSVYQQQA YANLLETLMP MVLKKAVDRS VALRRGLPLH TFQILGNAYK
ANDCGSRQLL VENVQKLVAK YLMPSEDDID EAVDQMAKKF QHEALPPIVL PSEEVRTVHG
ARSGADDQGN CVCDYKFNEK TSVRLLRANI LRLVTEPDGS VRIYHHVDNG LDYCKYEPYF
MEILPEKAKA VELLISAYPY YLTIDQLPLK SSARKVEVAT ALWEHGLLMT EKPFK
