NO66_DROWI
ID NO66_DROWI Reviewed; 767 AA.
AC B4NP88;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, 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=GK15670;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
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; CH964291; EDW86328.1; -; Genomic_DNA.
DR RefSeq; XP_002075342.2; XM_002075306.2.
DR AlphaFoldDB; B4NP88; -.
DR SMR; B4NP88; -.
DR STRING; 7260.FBpp0244813; -.
DR EnsemblMetazoa; FBtr0246321; FBpp0244813; FBgn0217675.
DR EnsemblMetazoa; FBtr0420072; FBpp0378195; FBgn0278910.
DR GeneID; 6652943; -.
DR KEGG; dwi:6652943; -.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_2_0_1; -.
DR InParanoid; B4NP88; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; B4NP88; -.
DR Proteomes; UP000007798; 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..767
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390993"
FT DOMAIN 420..565
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 21..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 466
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 468
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 531
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 767 AA; 85697 MW; 6B7DBB532C4E024D CRC64;
MDPETLDDLV NELFDKKKQL TVSQKQQREK LQAYMMAQLE GSSSASDDDD EDDGEGEDDN
DSNSDEDESG SESDATSADD SFSSDDNDDD DSGDEDGSDS GGSDSDLSFE DDSDYEDSHS
TEDLTEYTIN SENSSVEPTP PKRLKAGDKR PCSTQEEEES EDDNNNKPTA RKLQMGESAT
NGRIQQRKSM VEPATTSKPA SCPLTRKSLP ANGSAAKSCP LPPKNQKQSA AAKSCPLPPK
EKKLSSGAVA KSCPLPPKNE KPSSSGASCP LPSKTSKQVQ PRVCQLSDKP KSSSSQSTQK
RSKNEAAEGA TDTNGRQEAH RQNSIEEGRR ILSWVLNPIK PDDFFKDFWE KNACQVQRNA
PTYFSELISF EMIDQMMLKH HLEFTTNIDV TSYKDGRRET LNPEGRAMPP TVWGFYGEGC
SIRILNPSTY LPGLRTMCSL MQEFFHCLVG ANVYLTPPNS QGFAPHFDDI EAFVLQVEGR
KRWRLYMPLQ PSDVLARESS GNYTPDQLGE PIFDEVLKPG DVLYFPRGTV HQAITEKKHH
SLHITLSVYQ QQAYANLLEK LMPMVLQSAI KHSVSLRRGL PLHTWQHLGI AHGATKCSSR
SQLIKGIQEM VQQHLTPSEN QIDAAVDQLA KRYQHEALPP TILPEEKLRT VFGSRSATDA
HGKCLCDYEL TEDTSIRLLR ANILRLVVDE THLRVYYYVD NALEYCKYEA NFMEIEPTEA
AAVETLMHAY PAYVKISMLP LRKPERRIEV ATALWERGLL MTETPFK
