NO66_CAEBR
ID NO66_CAEBR Reviewed; 776 AA.
AC A8XEA2;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Jumanjic domain protein 1;
GN Name=jmjc-1; ORFNames=CBG11988;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE601540; CAP31037.1; -; Genomic_DNA.
DR RefSeq; XP_002646283.1; XM_002646237.1.
DR AlphaFoldDB; A8XEA2; -.
DR SMR; A8XEA2; -.
DR STRING; 6238.CBG11988; -.
DR EnsemblMetazoa; CBG11988.1; CBG11988.1; WBGene00033005.
DR GeneID; 8588280; -.
DR KEGG; cbr:CBG_11988; -.
DR CTD; 8588280; -.
DR WormBase; CBG11988; CBP09009; WBGene00033005; Cbr-jmjc-1.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_4_0_1; -.
DR InParanoid; A8XEA2; -.
DR OMA; PVFEGWI; -.
DR OrthoDB; 487605at2759; -.
DR Proteomes; UP000008549; Chromosome I.
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 GO; GO:0045471; P:response to ethanol; IEA:EnsemblMetazoa.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblMetazoa.
DR GO; GO:0006970; P:response to osmotic stress; IEA:EnsemblMetazoa.
DR GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblMetazoa.
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..776
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390980"
FT DOMAIN 425..569
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..203
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..285
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 470
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 535
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 776 AA; 88985 MW; 0F9B58C708F1CB65 CRC64;
MGKKNKSNGG GNTNNTPTKT PSKPPVKFND KWASIENGEA KSASVSHYKE PSKEPKFVHP
AKLAKEKKIF DGLDIPERVL AHGKVVEQNG GKKRRHREIS PKMEAKKPKV ESKSKDGVAA
KKAHKHFTVS SEVVQSTYFF EEPDNGNEVT LVSNGKETTI EKTVILDEEV EDEEIDEEEF
EDEEEVEDEE GMDEDETEID ESEMIVDPKD IERCIEFEDV DDEDEMEDEE EFEDEEEVED
EEVDDEEEEE VADEERGEEQ EDEQEEEEEV SDEESVVSEM DADSDDEGFI AGKDREAHVI
SKDKAARTFA AKPVDFDAFP FNDQDSVVTA SRAFGFMVSP CDVQTFFDKF YQSNVLVVHR
KTPAYYGNLF STTRFSELLE KHYLEYNMNI NIAQYKDGIR TTLNGKGRVY PQIVKQHLHN
LCSVQLVNPQ TFDDRIWYLC EILQEQFGCF VGANTYLTPA GSSGFAPHWD EIDAFLLQVE
GRKYWRVWAP ESAEEELPLE SSGNFTEDDM KGKEPVFEGW IEQGDMIYIP RGYTHQARTD
KKVHSLHVTV STGRQWSFAN LMEKVIPEAV GALTEERHKL RRGLPIGLFD MGGVVDLDYS
QEEHFTEKFK IVVDRHMSRL RNLVADHLLD SSVDSMTKEF MKQALPPILT DKEKKRSVIG
LSTNLLGDDL IDFCANTKVK FIRKHTQRLL MESEDSCFIS HRMNNSRLFE GRPETLVDFP
STGIDTYRVL WNAYPEWRTL DEIFSCRETK SNTRKEKLAA IQILFQMGVL LVKNPK
