NO66_DICDI
ID NO66_DICDI Reviewed; 514 AA.
AC Q54K96;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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;
DE AltName: Full=JmjC domain-containing protein G;
GN Name=jcdg; ORFNames=DDB_G0287513;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000102; EAL63656.1; -; Genomic_DNA.
DR RefSeq; XP_637159.1; XM_632067.1.
DR AlphaFoldDB; Q54K96; -.
DR SMR; Q54K96; -.
DR BioGRID; 1251163; 1.
DR STRING; 44689.DDB0233998; -.
DR PaxDb; Q54K96; -.
DR EnsemblProtists; EAL63656; EAL63656; DDB_G0287513.
DR GeneID; 8626160; -.
DR KEGG; ddi:DDB_G0287513; -.
DR dictyBase; DDB_G0287513; jcdG.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_4_0_1; -.
DR InParanoid; Q54K96; -.
DR OMA; EWGCMAG; -.
DR PhylomeDB; Q54K96; -.
DR Reactome; R-DDI-3214842; HDMs demethylate histones.
DR PRO; PR:Q54K96; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IBA:GO_Central.
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..514
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000348220"
FT DOMAIN 180..327
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 291
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 514 AA; 58748 MW; 8A4A0F5CC7DB0CAB CRC64;
MKRGLEEEIE EMSEEEVGVN NNNNGKKKKK KVVKKSKPVP LTKSVPQVSS QPLRPTKLVP
KKKTEIREIN INDIGSNELS VADQRVEADG VLAGLISPTI IEDFYDQYFG QKHLYVKRNG
DNIYKNFFTK DSLDKMLRNN LMKFTENVDV TNYVDFQRIT LNPEGRAYPS LVWKHYKEGC
SVRLLNPQTF NSNVWKLCST LQTHFQCGVG ANIYLTPAGA QGFAPHYDDV DVFILQLEGK
KEWRLYKPRD ANEVLPKKSS ENFTQEEIGE PYFTVTLEAG DLLYFPRGVI HQAVSPSDVH
SLHITVSTYL NNTWGDLIGK VLNRALEIAN EECLEFREGL PRDYTQYLGV IHSDKVGDER
RKELTDKVGT LWDKLGQLLP IDIGADQMAV KYLLDSLPPV LTQLEKKHSI EDETTSMKIK
PETRFRLIRA DSVRLVVEDI AILFHNADNT RIYHQVGEEP GVVEFTLECV DALEHIIDSY
PSYIYTKDLP IEDDDQKLDV VSALYEKGLI MFEK
