ID   A0A2K5NY42_CERAT        Unreviewed;       620 AA.
AC   A0A2K5NY42;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase {ECO:0000256|ARBA:ARBA00034525};
DE            EC=1.14.11.68 {ECO:0000256|ARBA:ARBA00034525};
GN   Name=KDM6B {ECO:0000313|Ensembl:ENSCATP00000042357.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000042357.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000042357.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-
CC         [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC         lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224,
CC         Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC         EC=1.14.11.68; Evidence={ECO:0000256|ARBA:ARBA00034421};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the UTX family. {ECO:0000256|ARBA:ARBA00034483}.
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DR   AlphaFoldDB; A0A2K5NY42; -.
DR   Ensembl; ENSCATT00000066792.1; ENSCATP00000042357.1; ENSCATG00000043776.1.
DR   GeneTree; ENSGT00940000160414; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000043776; Expressed in lung and 10 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032452; F:histone demethylase activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.1370; -; 1.
DR   Gene3D; 2.10.110.20; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR046941; KDM6_GATAL_sf.
DR   InterPro; IPR048562; KDM6A_B-like_C-hel.
DR   InterPro; IPR048560; KDM6A_B-like_GATAL.
DR   PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   PANTHER; PTHR14017:SF5; LYSINE-SPECIFIC DEMETHYLASE 6B; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF21322; KDM6_C-hel; 1.
DR   Pfam; PF21326; KDM6_GATAL; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT   DOMAIN          277..440
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  69514 MW;  4DFFBAEBE7A665B7 CRC64;
     LAPATSVPGK KAREEAPGPP GVSRADMLKL RSLSEGPPKE LKIRLIKVES GDKETFIASE
     VEERRLRMAD LTISHCAADV VRASKNAKVK GKFRESYLSP AQSVKPKINT EEKLPREKLN
     PPTPSIYLES KRDAFSPVLL QFCTDPRNPI TVIRGLAGSL RLNLGLFSTK TLVEASGEHT
     VEVRTQVQQP SDENWDLTGT RQIWPCESSR SHTTIAKYAQ YQASSFQESL QEEKESEDEE
     SEEPDSTTGT PPSSTPDPKN HHIIKFGTNI DLSDAKRWKP QLQELLKLPA FMRVTSTGNM
     LSHVGHTILG MNTVQLYMKV PGSRTPGHQE NNNFCSVNIN IGPGDCEWFA VHEHYWETIS
     AFCDRHGVDY LTGSWWPILD DLYASNIPVY RFVQRPGDLV WINAGTVHWV QATGWCNNIA
     WNVGPLTAYQ YQLALERYEW NEVKNVKSIV PMIHVSWNVA RTVKISDPDL FKMIKFCLLQ
     SMKHCQVQRE SLVRAGKKIA YQGRVKDEPA YYCNECDVEV FNILFVTSEN GSRNTYLVHC
     EGCARRRSAG LQGVVVLEQY RTEELAQAYD AFTLVRARRA RGQRRRALGQ AAGTGFGSPA
     APFPEPPPAF SPQAPASTSR
//