NO66_DROER
ID NO66_DROER Reviewed; 657 AA.
AC B3NU20;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=GG18702;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
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; CH954180; EDV45796.1; -; Genomic_DNA.
DR RefSeq; XP_001976869.1; XM_001976833.2.
DR AlphaFoldDB; B3NU20; -.
DR SMR; B3NU20; -.
DR STRING; 7220.FBpp0137248; -.
DR EnsemblMetazoa; FBtr0138756; FBpp0137248; FBgn0110911.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_2_1_1; -.
DR OMA; EWGCMAG; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; B3NU20; -.
DR Proteomes; UP000008711; 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 SMART; SM00558; JmjC; 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..657
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390985"
FT DOMAIN 315..454
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 357
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 420
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 657 AA; 73649 MW; 2596732EFB8D11D8 CRC64;
MQKASTSAGA KTAGNRKMQK SPNNGAAKAQ KSAKTVDTVT DSELLYNPPA FLTAAEKERR
KYLQARVRAE GESASTSSKS NATRPTDRKR HLQAEDPLPA DANNNDTNKG GKVAQESAST
QAAGTTKRKQ PRSQGLEQTS PIMVNGEALA CPLVRKSLPA AEAAKSCPLP SKKDSVTKSP
MTVHEAPKVD SATSNSNEKQ LATMPVDIHK TDSIEEGRRV LEWLINPVAV NQFFADFWEN
NACVVQRKNP NYYSKLMSFK MIDDILMRNR VEFGTNLDVT IYRNGKRETL NPEGRAFPSV
VWDFYAEGCS IRILNPSTYL LGLRQVCSIM QEFFHCLVGA NVYLTPPNSQ GFAPHYDDIE
AFVIQVEGRK RWRLYEPPEK ADQLSRTSSG NYDQKQLGEP IIDEVLEAGD LLYFPRGTVH
QAITEKGHFS LHITLSVYQQ QAYANLLETL MPIVLKKAVK KSVALRRGLP LHTFHVLGEV
QRTNRCESRD QLVENVQKLV SKYLMPSTQD IDEAVDQLAK KFQHEALPPI ILPEEKVRTV
FGSRSISDQE GNSVCDYEFD TDTSVRLLRA NILRLVNEDD GSVKIYHHVN NALEYCKYEP
NFLEILQEEA IAVEVLISAY PYYITVDQLP LKTVARKVEV ATALWEHGLL MTEKPFK
