NO66_DROVI
ID NO66_DROVI Reviewed; 907 AA.
AC B4M7P8;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=GJ17031;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH940653; EDW62815.1; -; Genomic_DNA.
DR RefSeq; XP_002057329.2; XM_002057293.2.
DR AlphaFoldDB; B4M7P8; -.
DR SMR; B4M7P8; -.
DR STRING; 7244.FBpp0231448; -.
DR PRIDE; B4M7P8; -.
DR EnsemblMetazoa; FBtr0232956; FBpp0231448; FBgn0204208.
DR GeneID; 6633376; -.
DR KEGG; dvi:6633376; -.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_2_0_1; -.
DR InParanoid; B4M7P8; -.
DR OMA; WERNACQ; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; B4M7P8; -.
DR Proteomes; UP000008792; 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..907
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390992"
FT DOMAIN 566..705
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..42
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 606
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 608
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 671
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 907 AA; 100776 MW; 192E89A9AFDFDF39 CRC64;
MADEVSAYAA YGKTLPKKQA PKRRQAKRWP KKTTKQTPKT LAKRTAKRAS GDKANGQNNG
AAAKRQNGVQ TKPKAQKLGT HDNASADARR IDSISGSIHC NGVNSNNNNN NSSSSSMPSK
KNKGRRSDVS DTEQSESLDD TVNLARKMAD YLSECGEQNC GSDADSSGSS YGEYDSSDND
DNMSGESGSA SESESCSEDY DKSSGSDSDN ECGDGDSDVD CDSDVDCDSD SEGGSAWGSE
SDDQFSEEYT LNSHANSSSN NNSSNNNSSS NNSNSSASSP EASVMPAAGR RKATKRSEHL
ASNSDGSDFI DSNNNNKNKN TPPAAKQQKL QVQQRLKQKQ LEKQEKRANA AVQRENAAPF
CPLQRTATTA AKSCPLPSKE AAGAKPGRKS CPLPSKSAPA ANKMAPNKMA AKMCALPPKN
ERAAQQQRKR AERDEQRQEA KGRRSENELL PEGKQRQQVH LQDSIEEGKR MLHWLINPMT
SDDFFSQYWE RNACQVKRKQ PNYFSQLISF KLIDEMLIRN HLEFTTNIDV TTYKNGMRET
HNPDGRAMPP TVWGFYSDGC SIRILNPSTY LIKVRQLCAM MQEFFHCLVG ANVYLTPPNS
QGFAPHYDDI EAFVLQVEGR KRWRLYSPLH PSDVLARNSS GNYSQAELGE PLFDAVLEPG
DILYFPRGTV HQAVCDQQQH SLHITLSVYQ QQAYANLLEE LMPAVLQRAI KHHLSLRRGL
PLHIWQHLGL AKGDQKSELR DELLGNTKRL VQQYLMPSDA QIDAAVDQLA KRFQHEALPP
VVLPEEHERT VFGSRSQANS HGQCLCDYEL TERTSVRLLR ANILRLVAEG SSLRVYYYVD
NALEFCKYEA NFMEIQPTEA AAVEALMSAY PKYLKVAKLP LRSAERRIEV ATALWERGLL
MTEQPFK
