ID A0A0V0S6Q5_9BILA Unreviewed; 695 AA.
AC A0A0V0S6Q5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
DE Flags: Fragment;
GN Name=KDM4E {ECO:0000313|EMBL:KRX22377.1};
GN ORFNames=T07_1342 {ECO:0000313|EMBL:KRX22377.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX22377.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX22377.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX22377.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX22377.1}.
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DR EMBL; JYDL01000032; KRX22377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0S6Q5; -.
DR STRING; 6336.A0A0V0S6Q5; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 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; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
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 Methyltransferase {ECO:0000313|EMBL:KRX22377.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Transferase {ECO:0000313|EMBL:KRX22377.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 20..62
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 154..315
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 466..577
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX22377.1"
SQ SEQUENCE 695 AA; 79641 MW; BD002674A62624A0 CRC64;
LFFGQLFVKS HHQLISLVME FTLSPSEEEF VNFPDYIATI DNDMWKEHGY VKVVAPEKWR
KSIVYDKTAI DNMTLEKINT QVLSGKKGVY NLENVAKNGT MSVTQFEKSV APYNRKILLK
PNMDTLASYE KTFWDKVTKG NLMYATDKLC SLFDENTNLW NISKLGTFLD KIVSFNGVTK
PYLYFGMMKS MFAWHTEDMD LPSINYLHYG YPKFWYVIPS AYKNDFDWLV SQYFPATALE
CEGFLRHKNI IFSHSKISSA GIPVRQVVQL PGEFILTYPG AYHSGFNLGF NCAEAVNFAM
KSWIDYSLKV KFCLCGHSTV RFDMVTVLDK LYRSGEINLE EMEKYYFENK STLHPGNSKL
VPYLKSTEPA VEKMETDSED YCVICRFFID GEQFFLQGRI PRDGTCVLSA LHFGDSVDVT
KKLDKLLCCS RCQVRVHARC YRCTDLSDDS DLAGWLCDVC KYQKGKVVCK LCGTSDTALL
EYKKSKFCHV QCALLSQNVR FVCPSSHGGQ KMIFQKAPLR GRCDYCDENK GTLIRCSEEN
CSAIFHLHCG RRLGVKYEVV DFLTNSKGIH ITCEAHSTKF ESYVNRRVIV QVSHGHKEMG
YVEDQYESIV YLVDFEDGCY SDVLDDDIVS CDCPNRNEKD HIHGVGARVV LNWIDGKSYR
VILRKASNEV CYSVMLEKTN SVIHVTRSDF TLAPE
//
