ID A0A3Q3SYG1_9TELE Unreviewed; 1425 AA.
AC A0A3Q3SYG1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000032830.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000032830.1}
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; ENSMAMT00000033682.2; ENSMAMP00000032830.1; ENSMAMG00000022092.2.
DR GeneTree; ENSGT00940000166518; -.
DR Proteomes; UP000261640; 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; 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; 2.
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:UP000261640};
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 1119..1282
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 20..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..560
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..961
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1425 AA; 155038 MW; 7BF1DF8B9AED2195 CRC64;
MQSCGVSLAV AACTAARSLG SASSSGDEGK KMAAGKASET EEDFPTLTAQ ERDSLVGIDS
SLFGFQKLHE DGARTKALLM KAVRCYDSLI LKAEGKVEPE LFCQLGHFNL LLEDYPKALS
AYQRYYSLQS DYWKNAAFLY GLGMVYFHYN AFQWAIKAFQ EVLYIDPGFS RAKEIHLRLG
LMFKVNTDYE SSLKHFQLAL IDSNPCTLSK AEIQFHIAHL YEIQKRYRAA KEAYEGLLQT
EDLPAQVKAT TLQQLGWMHH TVEQLGDRAS RDSYAIQCLQ KSLEADPNSG QSWYFLGRCY
SSIGKVQDAF ISYRQSIDKS EASADTWCSI GVLYQQQNQP MDALQAYICA VQLDHSHAAA
WMDLGTLYES CNQPHDAIKC YINATRSKGC TNTTALTHRI KCLQACKPNH SAEGGGSGPS
LPPHVGSLGP AEDQSCPAKR MRASSPAKSD SWASNPAQQP VPNWYLSPQK LQVLEQLRSN
RASLKPPQLQ MLEQLEAQLN MMQQHQHQMR QNASGGQVRP CLPNGPTTNS LPSPNPNLHP
LRPHLGPHRP PCPPQPLANG PVGPGAHRPL APLPVGDNSK NSSNNQPGPT AAGPNGDVPY
LQPVGSGDAA LLPHTCTSTQ TQDAAPCQAP HLNSSQGLQK GSVPHVTGSR SEGTPSHPQT
PNSTAPVHPN NQVGHSTNAP SPRQQPHNHL PSPPSLPPSS TSGGAAPGAS ATKDSNTTAT
PLGHGGSEGK TPSPLPSADG STVQVDGLTN HNHTGDGGKV VESGENPSLS ADNPKLPTLL
EEGKGPEEGE GPSQGTALKA STTPDSHKKV NNIHPAVLPS IPHAQGSSAA SSPISAISTA
TPSPKSSEHT QTGAHSPATN TSAAPAVNGN GKGGISEDSQ SPLKVEPPVV TSVKATPPHG
HSSSSSSSSS SVSIYPSSTN VLKACRNLGK NGLSNSSILL DKCPPPRLPP PPSPALPKDK
LNPPTPSIYL ENKRDAFFPP LHQFCTNPSN PVTVIRGLAG ALKLDLGLFS TKTLVEANPD
HLVEVWTQLS QPADENWDPT GTKKMWRCES ARAHTTIAKY AQYQAASFQE SLREENEKKA
LKEPSDTEPA SAESVARKRR GPLKHIKFGT NIDVSDERKW KQQLQELSKL PAFARVVSAG
NLLSHVGHTI LGMNTVQLYM KVPGSRIPGH QEHNNFCAVN INIGPGDCEW FAVPEPYWGV
MSNFCEKNNI NFLMGSWWPN LEDLYEADVP VYRFIQRPGD LVWLNTGTVH WVQAIGWCNN
IAWNVGPLTA HQYKLAVERY EWNKLQSVKS MVPMVHLSWN MARNIKVSDH KLFEMIKYCL
LRTLKQCQWV KEALASAGKE TVLRPRTRDE PAHYCTICEV EVFNLLFVRR ELLSKKQYVV
HCQDCARKGS ATLDDFVVLE QHRMEDLMQV YDQFTLAPPL HSSSS
//
