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NO66_DROAN
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   03-AUG-2022, entry version 69.
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.FBpp0123984; -.
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; 693909at2759; -.
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: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..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
 
 
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