ID A0A3B3HUU0_ORYLA Unreviewed; 1451 AA.
AC A0A3B3HUU0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=LOC101161131 {ECO:0000313|Ensembl:ENSORLP00000035128.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000035128.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000035128.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000035128.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000035128.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000035128.1};
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; ENSORLT00000028049.1; ENSORLP00000035128.1; ENSORLG00000004864.2.
DR GeneTree; ENSGT00940000166518; -.
DR OrthoDB; 20251at2759; -.
DR Proteomes; UP000001038; Chromosome 2.
DR Bgee; ENSORLG00000004864; Expressed in mesonephros and 13 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; -; 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; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 3.
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:UP000001038};
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 324..357
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1145..1308
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 17..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..987
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1451 AA; 157573 MW; C2FC547402437A24 CRC64;
MQSCGVSVAA AACAAARSLG SASSGGDEEK KMAAGKASET EEDFPTLTAQ EKDSLAGIDS
SLFGFQNLHE DGARTKGLLM KAVRCYDSLI LKAEGKVEPE LFCQLGHFNL LLEDYSKALS
AYQRYYSLQS DYWKNAAFLY GLGMVYFHYN AFQWAIKAFQ EVLYIDPGFS RAKEIHLRLG
LMFKVNTDYE SSLKHFQLAL IDSNPCTLSK AEIQFHIAHL YEIQKRYRAS KEAYESLLQT
EDLPPQVKAA TLQQLGWMHH TVEQLGDKAS RDSYAIQCLQ KSLEADPNSG QSWYFLGRCY
SSIGKVQDAF ISYRQSIDKS EASADTWCSI GVLYQQQNQP MDALQAYICA VQLDHSHAAA
WMDLGTLYES CNQPHDAIKC YINATRSKGC TNIAALTHRI KCLQAQLSNP QLSSLQGKSK
MLPLIEEAWS LPIPAELTSR QGGLSSAPQQ ACKPNHSAEG GASGQSLPPH VSSLGQTEDQ
SCPAKRRRAS GSSKSDSWGG NPAQQPAPNW NLSPQKLQML EQLRANKANL KPPQLQMLEQ
LEAQLAMMQQ LRQNASGGGQ LRPSLPNGPI INSLPSPNPS LHPTRFHLTP HRAPCPPQPL
SNGPVGSGTH SDSVGEGGSN NQLGPAAAGP NGDVPYLQAA DAGSSAAPLP HTCTSTQTQD
TAPRPALHLN SSQGLQKGCV PPASEETHLQ NPNSSTSVNP NNQVGHSTNA PSPRQPPHNH
LPSPPSIPHS STSSGAGPGA TKDDNTTATL VTAAPPLGNG SSESKPLVPP AEGAGAPADS
VANHILSGDA DKAAEGGDKP SLSADNPRLS ALLAGGKGPE EKEGLSEGAA STPVEPHRKV
NNIHPAVLPS TPHAQGSSAA SSPISAMSTA TPSPKSSEHN QTGGHSPSTA TPTAPAVNGK
GGISEDSQSP LKADPPASTC FKATPPHIHG SSSASSSISI YPSSTDVLKA CRNLGKNGLS
NSSILLDKCP PPRLPPPPSP ALPKDKLNPP TPSIYLENKR DAFFPPLHQF CTNPSNPVTV
IRGLAGALKL DLGLFSTKTL VEANPEHLVE VWTQLSQPAD ENWDPTGTKK MWRCESARSH
TTIAKYAQYQ ATSFQESLRE ENEKKALKEP SDTEPASAES AARKRRGPLK YIKFGTNIDV
SDERKWKQQL QELSKLPAFA RVVSAGNLLS HVGHTILGMN TVQLYMKVPG SRIPGHQEHN
NFCAVNINIG PGDCEWFAVP EPYWGVMSNF CEKNNINFLM GSWWPNLEDL YEADVPVYRF
IQRPGDLVWL NTGTIHWVQA IGWCNNIAWN VGPLIAHQYK LAVERYEWNK LQSVKSMVPM
VHLSWNMARN IKVSDHKLFE MIKYCLLRTL KQCQWVKEAL ATAGKETVLR TRTRDEPAHY
CTICEVEVFN LLFVRRELLT KKPYVVHCQD CARKGSATLD DFVVLEQYRM EDLMQVYDQF
TLAPPLHSAS S
//
