ID A0A3B4H5E9_9CICH Unreviewed; 1299 AA.
AC A0A3B4H5E9;
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:ENSPNYP00000028788.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000028788.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSPNYT00000029490.1; ENSPNYP00000028788.1; 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; 2.
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 999..1162
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..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..846
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1299 AA; 142299 MW; 065A6D5110E972CA 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 GGLSSAPQQV RDQIEQLTPP TPPSSPLLSL PPHVGSLGQA
DDQSCPAKRR KASGPAKVNM GDSWASNPAQ PVPNWYLSPQ KLQMLEQLRS NRANLKPPQL
QMLEQLEAQL AIMQQQQHQH QGSVPHGSSS EGTLSHPETP NSTTLAHPNN QVGHSTNAPS
PRPHNHLPSP PSLPHSSTSG GAGPSASATK DGNATAASLG NGNSVVKTPS PLPSADGKAA
QGDGLANHIH SDGGKVVEGG DKPSLSADNP RLSALLAGGK GTAPAASTTS DPHKKINNIH
PAVLPSTPHA QGSSAASSPI SAISTATPSP KSSEHTQACG HSPAGTAATA PAVNGNSKGA
TPPHGHSSSS SSSSSSISIY PSSTDVLKAC RNLGKNGLSN SSILLDKCPP PRLPPPPSPA
LPKDKLNPPT PSIYLENKRD AFFPPLHQFC TNPSNPVTVI RGLAGALKLD LGLFSTKTLV
EANPEHLVEV WTQLSQPADE NWDPTGTKKM WRCESARSQT TIAKYAQYQA ASFQESLREE
NEKKALKEPS DTEPASAERY LSAFFNKDPG LIILALLQKW KQQLQELSKL PAFARVVSAG
NLLSHVGHTI MGMNTVQLYM KVPGSRIPGH QEHNNFCAVN INIGPGDCEW FAVPEPYWGV
MSNFCEKNNI NFLMGSWWPN LEDLYEADVP VYRFIQRPGD LVWLNTGTVH WVQAIGWCNN
IAWNVGPLTA HQYKLAVERY EWNKLQSVKS MVPMVHLSWN MARNIKVSDH KLFEMIKYCL
LRTLKQCQWV KEALAAAGKE TVLRPRTRDE PAHYCTICEV EVFNLLFVRR ELLSKKQCVV
HCQDCARKGS AALDDFVVLE QYRMEDLMQV YDQFTLVSR
//
