ID A0A673X4W8_SALTR Unreviewed; 879 AA.
AC A0A673X4W8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN Name=LOC115192313 {ECO:0000313|Ensembl:ENSSTUP00000019204.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000019204.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000019204.1}
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; A0A673X4W8; -.
DR Ensembl; ENSSTUT00000020200.1; ENSSTUP00000019204.1; ENSSTUG00000007725.1.
DR GeneTree; ENSGT00940000154930; -.
DR Proteomes; UP000472277; 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; cd20463; Tudor_JMJD2A_rpt1; 1.
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); 1.
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; IPR047479; Tudor_KDM4A_rpt1.
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:SF51; [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:UP000472277};
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 581..707
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 357..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 100303 MW; 2453D46E8C460CEB CRC64;
MATDTASQQT PGSKIMTFHP SMEEFKDFSR YIAYMESQGA HRAGMAKVIS PKDWKPRRTY
DDIDDLVIPA PIQQVVTGQS GLFTQYNIQK KPMTVREFRK TANTDKFCNP RYVDFDELER
KFWKNLTFNP PLYGADVNGT LYDPDVTEWN IGHLNTILDT VERESGIKIK GVNTPYLYFG
MWKSTFAWHT EDMDLYSINY LHFGEPKSWY VVPPEHGKRL ERLAKGFFPG SAQSCEAFLR
HKMTLISPSI LKKYGIPFEK ITQEAGQFIV TFPFGYHAGF NHGFNCAEST NFATQRWIDY
GKIATLCSCR KDMVKISMDV FVRKFQPDRY KAWKAGKDNI PIDHSKPTPE AAEFLTGEKT
GEPGKEGPSP SEAPDQEEDT PGTTAQEETR SVHYCTHLPC HVYSEDEGVQ SKLGKLPRHH
PLMKDSMSDE ELPEQPPVEE DGLEGELWAK PFVHLWQNRP PSLKREKEYN RRMGLQAPYC
SVCSLFQTYQ RVRKERRVEE SDTPVVLPGG RLRTKPLIAE MCFTTTTEPE EGAEEQALGA
LAPTTPHLEP DGTSLLISCS HCSVRIHTSC YGVDPKIVTK DWKCARCKAN AMTEVTTNNG
MFLCVLTCFC VCYRWVHVLC AVAVLEARFV NITERSPVDL SGIPLQRFKL KCYYCKKRMK
KTSGCCVQCS HGRCSTAYHP TCAQAAGVLM QPDEWPFVVY VTCCRHKGPI QTELTVGQRV
ICKHKNGRYY QCDVVQLSKE TFYEVNFDDG SFSDNLFPED IVSRNCAQLG PPPQGEVVQV
RWTDGLVYGA KFVAAHIIQM YQVEFEDGSQ LTAKRDDVYT LDEELPKRVK SRLSKASDMR
FDGIFEDKEA IQQSKRQRVI NSRYRGDYIE PVIYRAIME
//
