NO66_CULQU
ID NO66_CULQU Reviewed; 648 AA.
AC B0WMG3;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-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=CPIJ008401;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB;
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; DS231997; EDS31020.1; -; Genomic_DNA.
DR RefSeq; XP_001849897.1; XM_001849845.1.
DR AlphaFoldDB; B0WMG3; -.
DR SMR; B0WMG3; -.
DR STRING; 7176.CPIJ008401-PA; -.
DR PRIDE; B0WMG3; -.
DR GeneID; 6040511; -.
DR KEGG; cqu:CpipJ_CPIJ008401; -.
DR VEuPathDB; VectorBase:CPIJ008401; -.
DR VEuPathDB; VectorBase:CQUJHB008294; -.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_4_1_1; -.
DR InParanoid; B0WMG3; -.
DR OMA; EWGCMAG; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; B0WMG3; -.
DR Proteomes; UP000002320; Partially assembled WGS sequence.
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..648
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390983"
FT DOMAIN 308..453
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 356
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 419
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 648 AA; 73041 MW; FF7C1EAB101FF44E CRC64;
MSKVSSIFDT PAPDPRPATT ENGAAAKPAA RKKKSPAAAT KKQLIDQLIR EMSQDEDNND
SVDQAPPAKK SRKKADSSGN NNTSKSSVKD KPAKPKKPKT AGLKIKLQDH RKHKEKLRKS
LQGVENSRQA AASTSMLEAS FNGDSLKDRS NHSTPVHHKG AKAAKKNKNK SHIMPLPLTF
TPSKVVVKQE PKTPRRPTML NVEASSGSLD SVEIGREKFS WVIGPSTTVD EFMAQFWEKK
PFLVQRNDPT YYANLLSRGK IDEMLRNNNI EYTKNLDVTS YREGVRETHN PDGRALPPDV
WAFYEEGCSI RMLNPQTYLP GVYEMNVKLQ EFFHCMTGSN FYLTPPNSQG FAPHYDDIEA
FVLQVEGRKH WKLYSPRTAS EVLARVSSPN FTQEEIGVPI LEVTLEPGDL LYFPRGIIHQ
ASTVPGHHSL HVTMSVYQKN SWADLLELYL PHALSQAAEN HLELRRGIPQ DLHQHFGIVH
SDNETPTRKD LIKKIKSLVD KIFSEEAIDV AVDQLAKRFQ HDALPPLLTD QERAQTAYGA
NYAFNPDGTV PLQTAFTERT TIRLLRRNIV RLVNEENTLR LYYHTENSRE YHEYEPNFLE
VDQDAALGVE LLVKIYPETV AIGALPVEDK VEFAKSLWEK GLIVARGE
