ID A0A3P8T8C5_AMPPE Unreviewed; 1152 AA.
AC A0A3P8T8C5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000021670.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000021670.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000021670.1}
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(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, 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=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00000040};
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 JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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DR AlphaFoldDB; A0A3P8T8C5; -.
DR Ensembl; ENSAPET00000022245.1; ENSAPEP00000021670.1; ENSAPEG00000015450.1.
DR GeneTree; ENSGT00940000154930; -.
DR OMA; SGQYDMT; -.
DR Proteomes; UP000265080; Chromosome 10.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20466; Tudor_JMJD2A_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.10.330.70; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047481; Tudor_KDM4A_rpt2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694:SF142; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 15..57
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 143..309
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 859..973
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 420..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1152 AA; 131470 MW; 393874C2FE9D3895 CRC64;
MASDVVSQNH GTKGIVTFYP TAAEFKDFSR YIAYMESQGA HKAGLAKIVP PKEWKPRSSY
DDIDNLVIPA PIQQVVTGQS GLFTQYNIQK KSMAVREFRK IANSDKFCSP HYDDFEELER
KYWKNVTFNP PIYGADVNGT LYDPDVKEWN ICHLDTILDT VERDSGITIE GVNTPYLYFG
MWKTTFAWHT EDMDLYSINY LHFGEPKSWY CVPPEHGKRL ERLAKGFFPG SAQNCEAFLR
HKMTLISPSI LKKYGIPFEK ITQEAGEFMV TFPYAYHAGF NHGFNCAEST NFATERWIEY
GKQAVLCSCR KDMVKISMDV FVKKFQPDRY EHWLAGRDVV PIDHSRPTPE AKEFLGESFN
DITSSSYSSS IEGCWEDGER KSTTQRIETK RHRVYLELPE EVVPKDEDDD VVAQYGKRPR
LSLIPPRTTS QDGKRNKGPP KLVVTPTKLT LMDPFHRGLT QSNSDGGRPP HYTKTRAPAI
SSQSQHRNGH LSISLAPMWT EVAAQPARKM GVASLLFHRT LSPKDTLQVH SYTLEKQRQP
HTQLQVHSYA REHQPRHLQH KACTPSHTQV QSSSQAPSCE RTEPQMESKI VVTKVAQNES
EAQKPVVQEQ EETKPKVLIP VESQAGVEKT EVVPTVTSAP PHTQTQSQDL SNEKMEAPKN
NKRKVSEEQS YCKSLVSKQQ QQEEELCKLP RHHPLIRELH SDDDVYVDVE VEQEEKEEWA
KPLTQLWQCR PYNPEAERKY NKSMGQQAPY CSICLLFHTY HQSESTSASS TLTLVNRPGG
QQWSRPLIPE MCFNTQSNKT TDSGEGQLSN PHVAEDGTSR LVSCAQCCVR VHTSCYGVSG
DEEELDDWLC ARCEADAITE DCCLCSLRGG ALQRANNDRW VHVLCAITVL EARFVNITER
SPIDLSAIPL PRFRLKCAYC RKRMKREVKG CCVQCSHGRC STAFHPTCAQ AAGILMHPDD
WPFVVFITCH RHRTPVIPER NKASMRELAV GQKVICKYKN GRYYHSDVVE LTTATFYEVV
FDDGSYSDNL FPEDIENRDC VRLGPPSEGD VVQVRWTDGL IYGAKFVASH SIPMYLVEFE
DGSQITVKRE DIYTLDEDLP KRVKSRMSVA SDMRFELFAQ SDVKQNSKRQ RVINSRYRED
YIEPVIYRAI ME
//
