NO66_DROGR
ID NO66_DROGR Reviewed; 723 AA.
AC B4JMQ2;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=GH24285;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916371; EDV91995.1; -; Genomic_DNA.
DR RefSeq; XP_001992288.1; XM_001992252.1.
DR AlphaFoldDB; B4JMQ2; -.
DR SMR; B4JMQ2; -.
DR STRING; 7222.FBpp0158191; -.
DR PRIDE; B4JMQ2; -.
DR EnsemblMetazoa; FBtr0159699; FBpp0158191; FBgn0131741.
DR GeneID; 6565600; -.
DR KEGG; dgr:6565600; -.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_2_0_1; -.
DR InParanoid; B4JMQ2; -.
DR OMA; IRFQHEA; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; B4JMQ2; -.
DR Proteomes; UP000001070; 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; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..723
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390986"
FT DOMAIN 379..518
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 13..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 419
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 421
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 484
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 723 AA; 80068 MW; 861058AE03777B6B CRC64;
MDEMSAYVAY GMKKTAKKPA KKTTKQNRQK QKAANIYSLA TSTPAKISAV KQNNGAKGKA
KANGVKGNAK AQTTKDSATN SVAKMADESV DDYSSDSSYD EDEDNEELSH SSNEDDYGSE
LSSGEEFEEY TLNSPSGSCS CSASSGSSNT ENSPPAATSS RTPKKRSTGD MDDNNNKSPA
VKQQKLQPQE QKEGKELSKK GSRKSAPAAA PSCPLLRLSG NAAAIKSSAM PSKATAEKRK
SCPLPKKMAA AGKGVAVVKQ EPKAKVESVQ NGGVEDSVER GICVLGALLD PLSLDDFFSR
YWESKACQVK RKRKDLYSDL VSFEMIDEML IENHLEFTTN IDVTSYKDGV RQTHNPDGRA
MPPTVWGHYS DGCSVRILNP STYLKGLRGV CAALQEHFHC LVGANVYLTP PNSQGFAPHY
DDIEAFVLQV EGRKRWRLYD APSPNDVLAR TSSGNLKQQQ LSKPIFDEVL EAGDLLYFPR
GCVHQAVTEQ QHHSLHITLS VYQQQSYANL MEALMPAVLQ NAIKHNLDMR RGLPLGTWHH
LGMVHGDKKT KERSDLITHT QSLFSKYLAP TASQIDAAVD QLAIRFQHEA LPPRIASSEK
KRTVFGSRNK KDKHGNCRCD YDLTEQTKIR LLRQNIVRLV AQEENSLRLY YYVDNALEYC
KYEANFMEID RVEANAIKML INSYPKYVSI SSLPLPNVEH CLDTATGLWE RGLLITEEPF
KKN
