ID A0A3B4GZL9_9CICH Unreviewed; 1390 AA.
AC A0A3B4GZL9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000028370.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000028370.1}
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000256|ARBA:ARBA00034483}.
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DR Ensembl; ENSPNYT00000029061.1; ENSPNYP00000028370.1; ENSPNYG00000017996.1.
DR GeneTree; ENSGT00940000166518; -.
DR Proteomes; UP000261460; 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 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 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 1084..1247
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 504..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..926
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1390 AA; 151508 MW; EC8A1907E81557EB 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
DLPAQVKATT LQQLGWMHHT VEQLGDRGSR DSYAIQCLQK SLEADPNSGQ SWYFLGRCYS
SIGKVQDAFM SYRQSIDKSE ANADTWCSIG VLYQQQNQPM DALQAYICAV QLDHSHAAAW
MDLGTLYESC NQPHDAIKCY INATRSKGCT NTAALTHRIK CLQAQLSNPQ LSSLQSKSKM
LPLIEEAWSL PIPAELTSRQ GGLSTKCYPS GDSWASNPAQ PVPNWYLSPQ KLQMLEQLRS
NRANLKPPQL QMLEQLEAQL AIMQQQQHQQ SASGGQVRPS LPNGPTTNSL PSPNPSLHPM
RPHLGPHRPP CPPQPLANGP VGSAPHGHSD PLPAGDSSNS SSNSSSSNNN QPGPAPTGPN
GDVPYLQPAG SGGAALLPHT CTNTQTQDAM PRQALHLNSS QVRRLTDGLC SLLFFIPALV
TEPALLSAAV LRPSASATKD GNATAASLGN GNSVVKTPSP LPSADGKAAQ GDGLANHIHS
DGGKVVEGGD KPSLSADNPR LSALLAGGKG PEESEGPSEG TAPAASTTSD PHKKINNIHP
AVLPSTPHAQ GSSAASSPIS AISTATPSPK SSEHTQACGH SPAGTAATAP AVNGNSKGGI
SEDSQSPLKA EPPAVTSLKA TPPHGHSSSS SSSSSSISIY PSSTDVLKAC RNLGKNGLSN
SSILLDKCPP PRLPPPPSPA LPKDKLNPPT PSIYLENKRD AFFPPLHQFC TNPSNPVTVI
RGLAGALKLD LGLFSTKTLV EANPEHLVEV WTQLSQPADE NWDPTGTKKM WRCESARSQT
TIAKYAQYQA ASFQESLREE NEKKALKEPS DTEPASAESA ARKRRGPLKY IKFGTNIDVS
DERKWKQQLQ ELSKLPAFAR VVSAGNLLSH VGHTIMGMNT VQLYMKVPGS RIPGHQEHNN
FCAVNINIGP GDCEWFAVPE PYWGVMSNFC EKNNINFLMG SWWPNLEDLY EADVPVYRFI
QRPGDLVWLN TGTVHWVQAI GWCNNIAWNV GPLTAHQYKL AVERYEWNKL QSVKSMVPMV
HLSWNMARNI KVSDHKLFEM IKYCLLRTLK QCQWVKEALA AAGKETVLRP RTRDEPAHYC
TICEVEVFNL LFVRRELLSK KQCVVHCQDC ARKGSAALDD FVVLEQYRME DLMQVYDQFT
LAPPLHSSSS
//
