ID I3K2A9_ORENI Unreviewed; 1434 AA.
AC I3K2A9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase {ECO:0000256|ARBA:ARBA00034525};
DE EC=1.14.11.68 {ECO:0000256|ARBA:ARBA00034525};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000015254.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000015254.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000256|ARBA:ARBA00034483}.
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DR Ensembl; ENSONIT00000015267.2; ENSONIP00000015254.2; ENSONIG00000012116.2.
DR GeneTree; ENSGT00940000166518; -.
DR HOGENOM; CLU_003187_0_0_1; -.
DR Proteomes; UP000005207; Linkage group LG23.
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 SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 4.
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:UP000005207};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 99..132
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 136..169
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 289..322
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 323..356
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1128..1291
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 18..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..609
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..995
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1434 AA; 156003 MW; 7AF577A634A45448 CRC64;
MQSCGVSLAA AACAAARSLG SASSSGDEGK KMAAGKASET EEDFPTLTAE ERDSLAGIDS
SLFGFQKLHE DGARTKALLM KAVRCYDSLI LKAEGKVDPE LFCQLGHFNL LLEDYPKALS
AYQRYYSLQS DYWKNAAFLY GLGMVYFHYN AFQWAIKAFQ EVLYIDPGFS RAKEIHLRLG
LMFKVNTDYE SSLKHFQLAL IDSNPCTLSK AESKHLFYLF ECYKKYRASK EAYESLLQTE
DLPVQVKATT LQQLGWMHHT VEQLGDRASR DSYAIQCLQK SLEADPNSGQ SWYFLGRCYS
SIGKVQDAFM SYRQSIDKSE ANADTWCSIG VLYQQQNQPM DALQAYICAV QLDHSHAAAW
MDLGTLYESC NQPHDAIKCY INATRSKGCT NTAALTHRIK CLQAQLSNPQ LSSLQSKSKM
LPLIEEAWSL PIPAELTSRQ GGLSSAPQQA CKPNHSAEGG GSGQSLPPHV GSLGQADDQS
CPAKRRKASG PAKVNMAVVS LVVSRVIIIF RCHMVLTLSV RLQMLEQLRS NRANLKPPQL
QMLEQLEAQL AIMQQHQHQT ERLRRSGAPI SSQRPHYQLP PSPNPSLHPM RPHLGPHRPP
CPPQPLANGP VGSAPHGHSD PLPAGDSSNS SNSSSSNNNQ PGPAPTGPNG DVPYLQPAGS
GSAALLPHTC TNTQTQDAMP RQALHLNSSQ GLQKGSVPHG SSSEGTLSHP ETPNSTTLAH
PNNQVGHSTN APSPRPHNHL PSPPSLPHSS TSGGAGPSVS ATKDGNATAA SLGNGNSEVK
TPSPLPSADG KAAQGDGLAN HIHSDGGKVV EGGDKPSLSA DNPRLSALLA GGKASTTSDS
HKKINNIHPA VLPSTPHAQG SSAASSPISA ISTATPSPKS SEHTQTGGHS PAATAATAPA
VNGNSKGGIS EDSQSPLKAE PPAVTSLKAT PPHGHSSSSS SSSSSISIYP SSTDVLKACR
NLGKNGLSNS SILLDKCPPP RLPPPPSPAL PKDKLNPPTP SIYDWPELSN WVNGSITNLQ
LCAGVFLHAD LGLFSTKTLV EANPEHLVEV WTQLSQPADE NWDPTGTKKM WRCESARSQT
TIAKYAQYQA ASFQESLRVS STFAARKRRG PLKYIKFGTN IDVSDERKWK QQLQELSKLP
AFARVVSAGN LLSHVGHTIM GMNTVQLYMK VPGSRIPGHQ EHNNFCAVNI NIGPGDCEWF
AVPEPYWGVM SNFCEKNNIN FLMGSWWPNL EDLYEADVPV YRFIQRPGDL VWLNTGTVHW
VQAIGWCNNI AWNVGPLTAH QYKLAVERYE WNKLQSVKSM VPMVHLSWNM ARNIKVSDHK
LFEMIKYCLL RTLKQCQWVK EALAAAGKET VLRPRTRDEP AHYCTICEVE VFNLLFVRRE
LLSKKQCVVH CQDCARKGSA ALDDFVVLEQ YRMEDLMQVY DQFTLAPPLH SSSS
//
