ID A0A3Q1G326_9TELE Unreviewed; 1152 AA.
AC A0A3Q1G326;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000012735.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000012735.1}
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(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; A0A3Q1G326; -.
DR Ensembl; ENSAPOT00000032126.1; ENSAPOP00000012735.1; ENSAPOG00000015433.1.
DR GeneTree; ENSGT00940000154930; -.
DR Proteomes; UP000257200; Unplaced.
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:UP000257200};
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 364..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..667
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 604..618
FT /note="Basic and acidic 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; 131212 MW; 13BBE510FB14FF85 CRC64;
MASDVVSQNH GTKGIMTFYP 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
DITSGSHSSS IDGCGEDGER KSTTQRIETK RHRVCLELPK EVVPKDEDED VVAQYGKRPR
LSLIPPRTIL QDGKRNKGPP KLVVTPTKLT LMDPFHRGLT QGNSDGGRPP HYTKTRAPAI
SSQSQHRNGH LSISVAPMWT EAAAQPARKM GVASLLFHRT LSPKDALQVH SYTLEKQRQP
HTQLQVHSYA REHQPRHLQH KVCTPSHTQV QSSSQAPSCE RTEPQLESKV VVTKVAQKES
EAQKPVVQEQ EETKPKVLRP VESQAGVAKT EVKPTVTSAP PHTQTQSQDF SNEKMEAPKN
SKRKQVSEEQ SYCKSLVSKQ QQQEELCKLP RHHPLIRELH SDDDMYVDVE VEQEEKEEWA
KPLSQLWQCR PYNPEAERKY NKSMGQQAPY CSICLLFHTY HQSESTSVSS TLTLVKRPGG
QQWSKPLIPE MCFNTQSNKT SDSGEGQLSN PHVAEDGTSR LVSCAQCCVR VHTSCYGVSG
DEEDLDDWLC ARCEADAVTE DCCLCSLRGG ALQRANNDRW VHVLCAITVL EARFVNITER
SPIDLSAIPL PRFRLKCAYC RKRMKREVKG CCVQCSHGRC STAFHPTCAQ AAGVLMHPDD
WPFIVFITCH RHRTPVIPER NKASMRELAV GQKVICKYRN GRYYHSDVVE LTTATFYEVV
FDDGSYSDNL FPEDIENRDC VRLGPPSEGD AVQVRWTDGL IYGAKFIASH SIPMYLVEFE
DGSQITVKRE DIYSLDEDLP KRVKSRMSVA SDMRFELFAQ SDVKQNSKRQ RVINSRYRED
YIEPVIYRAI ME
//
