ID NO66_DROAN Reviewed; 843 AA.
AC B3MSI4;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=GF20792;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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; CH902622; EDV34739.1; -; Genomic_DNA.
DR RefSeq; XP_001964290.1; XM_001964254.2.
DR AlphaFoldDB; B3MSI4; -.
DR SMR; B3MSI4; -.
DR STRING; 7217.B3MSI4; -.
DR EnsemblMetazoa; FBtr0125492; FBpp0123984; FBgn0097798.
DR GeneID; 6503484; -.
DR KEGG; dan:6503484; -.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_2_0_1; -.
DR InParanoid; B3MSI4; -.
DR OMA; CKYDANF; -.
DR OrthoDB; 5491189at2759; -.
DR PhylomeDB; B3MSI4; -.
DR Proteomes; UP000007801; 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:0051864; F:histone H3K36 demethylase activity; ISS:UniProtKB.
DR GO; GO:0140680; F:histone H3K36me/H3K36me2 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR Gene3D; 3.90.930.40; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 1.10.10.1500; JmjC domain-containing ribosomal oxygenase (ROX), dimer domain; 1.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR039994; NO66-like.
DR InterPro; IPR049043; RIOX1/NO66-like_C_WH.
DR PANTHER; PTHR13096; MINA53 MYC INDUCED NUCLEAR ANTIGEN; 1.
DR PANTHER; PTHR13096:SF10; RIBOSOMAL OXYGENASE 1-RELATED; 1.
DR Pfam; PF08007; JmjC_2; 1.
DR Pfam; PF21233; RIOX1_C_WH; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 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..843
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390984"
FT DOMAIN 502..641
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 542
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 544
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 607
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 843 AA; 91763 MW; 31C325362F995DDD CRC64;
MSRNQRDSGK AAVDAKINGK PQTNGGAKRG PKIPKDNSKK KKAPPSNTTP TTNQTNLDKL
VNQLYDKNSK QGMPQKQQRK KLQEYLSAQV QGTDSATSSS SASGLAPNSF SDSSASEESS
DDELGDMTSP SSSSSLSASD SDEMSEYTLS SSTPEVPAIA KTSGARAELK RRNKEKEALA
ADPNNNRAPP AKNKNAAEGP GPASSNPRIQ RRVTMAGDLV HTEPVTGETG ALHCPLKRKS
VASCPLPAKA KSPNPTQPAK AAPESKAAGS AKSKAPVVPR LKEDAKNKPG PSARGVSPAV
DIEITSCISL PSTAGLPASG SKSPAAGKIS PKPGTSASAK PSTSASAKPS TSKSSAKSSS
DKSNDAAASG PTTSAPAKKK EESSKSGDKA KSKDYHKVNS IEEGRRILQW ILNPVQPDEF
FGSFWEKNAC QVQRQTPKYF AELISFEMID EMLIRHHLEF TTNIDVTTYK DGVRQTLNPE
GRAMPPAVWS SYADGCSIRI LNPSTYLAGL RQVCSMLQEF FHCLVGANVY LTPPNSQGFA
PHYDDIEAFV LQVEGRKRWR LYMPVKPTDM LARHSSGNFD QGELDEPIFD EVLEAGDVLY
FPRGTVHQAI TEKDQHSLHI TLSVYQQQAY ANLLENLMPM VLKNAVQQKM ALRRGLPLHT
WQNLGLAHGG SEGRSRLNLI SGIQQMVQKY LLPTEEQIDA AVDQLAKRFQ HEALPPTILP
EERVRTVFGS RSQTDAQGQC LCDYEITEQT SVRLLRANIL RLVAEEGILR LYYYVDNALE
YCKYDANFME IEPTEAAAVE MLLHSYPAYI KVGQLPLHSG DRRVDVATAL WERGLLMTEK
PFK
//
