ID A0A2K6V2K7_SAIBB Unreviewed; 1384 AA.
AC A0A2K6V2K7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=KDM6A {ECO:0000313|Ensembl:ENSSBOP00000038412.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000038412.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000038412.1}
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 Ensembl; ENSSBOT00000055363.1; ENSSBOP00000038412.1; ENSSBOG00000033677.1.
DR GeneTree; ENSGT00940000155202; -.
DR Proteomes; UP000233220; Unplaced.
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; -; 2.
DR Gene3D; 2.10.110.20; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR14017:SF9; LYSINE-SPECIFIC DEMETHYLASE 6A; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21322; KDM6_C-hel; 1.
DR Pfam; PF21326; KDM6_GATAL; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 2.
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:UP000233220};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 106..139
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 294..327
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1078..1241
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 406..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..920
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1384 AA; 152582 MW; 5F53526C3823576E CRC64;
MAAGKASGES EEASPSLTAE EREALGGLDS RLFGFVRFHE DGARTKALLG KAVRCYESLI
LKAEGKVESD FFCQLGHFNL LLEDYPKALS AYQRYYSLQS DYWKNAAFLY GLGLVYFHYN
AFQWAIKAFQ EVLYVDPSFC RAKEIHLRLG LMFKVNTDYE SSLKHFQLAL VDCNSCTLSN
AEIQFHIAHL YETQRKYHSA KEAYEQLLQT ENLSAQVKAT VLQQLGWMHH TVDLLGDKAT
KESYAIQYLQ KSLEADPNSG QSWYFLGRCY SSIGKVQDAF ISYRQSIDKS EASADTWCSI
GVLYQQQNQP MDALQAYICA VQLDHGHSAA WMDLGTLYES CNQPQDAIKC YLNATRSKSC
SNTSALAARI KYLQACKPHH PNTEPVLGLS QTPISQQSLP LHMIPSSQVD DLSSPAKRKR
TSSPTKNTSD NWSGGHAVSH PPVQQQAHSW CLTPQKLQHL EQLRANRNNL NPAQKLMLEQ
LESQFVLMQQ HQMRPTGVAQ VRSTGIPNGP TADSSLPTNS VSGQQPQLAL TRVPSVSQPG
VRPACPGQPL ANGPFSAGHV PCSTSRTLGS TDTILIGNNH VTGSGSNGNV PYLQRNALTL
PHNRTNLTSS AEEPWKNQLS NSTQGLHKGQ SSHSAGPNGE RPLSSTGPSQ HLQAAGSGIQ
NQNGHPTLPS NSVTQGAALN HLSSHTATSG GQQGITLTKE SKPSGNILTV PETSRHAGET
PNSTASVEGL PNHVHQMTAD AVCSPSHGDS KSPGLLSSDN PQLSALLMGK ANNNVGTGTC
DKVNNIHPAV HTKTDNSVAS SPSSAISTAT PSPKSTEQTT TNSVTSLNSP HSGLHTINGE
GMEESQSPMK TDLLLVNHKP SPQIIPSMSV SIYPSSAEVL KACRNLGKNG LSNSSILLDK
CPPPRPPSSP YPPLPKDKLN PPTPSIYLEN KRDAFFPPLH QFCTNPSNPV TVIRGLAGAL
KLDLGLFSTK TLVEANNEHM VEVRTQLLQP ADENWDPTGT RKIWHCESNR SHTTIAKYAQ
YQASSFQESL REENEKRSHH KDHSDSESTS SDNSGRRRKG PFKTIKFGTN IDLSDDKKWK
LQLHELTKLP AFVRVVSAGN LLSHVGHTIL GMNTVQLYMK VPGSRTPGHQ ENNNFCSVNI
NIGPGDCEWF VVPEGYWGVL NDFCEKNNLN FLMGSWWPNL EDLYEANVPV YRFIQRPGDL
VWINAGTVHW VQAIGWCNNI AWNVGPLTAC QYKLAVERYE WNKLQSVKSI VPMVHLSWNM
ARNIKVSDPK LFEMIKYCLL RTLKQCQTLR EALIAAGKEI IWHGRTKEEP AHYCSICEVE
VFDLLFVTNE SNSRKTYIVH CQDCARKTSG NLENFVVLEQ YKMEDLMQVY DQFTLAPPLP
SASS
//
