ID A0A0V0TCR7_9BILA Unreviewed; 698 AA.
AC A0A0V0TCR7;
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};
GN Name=KDM4E {ECO:0000313|EMBL:KRX36795.1};
GN ORFNames=T05_381 {ECO:0000313|EMBL:KRX36795.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX36795.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX36795.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX36795.1};
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:KRX36795.1}.
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DR EMBL; JYDJ01000344; KRX36795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TCR7; -.
DR STRING; 144512.A0A0V0TCR7; -.
DR Proteomes; UP000055048; 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; 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:KRX36795.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Transferase {ECO:0000313|EMBL:KRX36795.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 23..65
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 157..318
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 469..580
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
SQ SEQUENCE 698 AA; 80470 MW; 0CE5146D9FA93EF9 CRC64;
MMWFFGYQYP ENHKALLISL AMEFTLSPSE EEFVNFPDYI ATIDNNMWKE HGYVKVVAPE
KWRKSIVYDK TAIDNMTLEK INTQVLSGKK GVYNLENIQK DGTMSVMQFE KSVAPHNRKV
LLKPNMDTVK SYEKMFWDKV TKGNLMYATD KLCSLFDENT NLWNISKLGT FLDKIVSFNG
VTKPYLYFGM MKSMFAWHTE DMDLPSINYL HYGYPKFWYV IPSAYKNDFD WLVSQYFPAT
ALECDGFMRH KNIIFSHSKI SSAGIPVRQV VQLPGEFILT YPGAYHSGFN LGYNCAEAVN
FAMKSWIDYS LKVKFCLCGH STVRFDMVTV LDKLYRSGEI NLEEMEKYYF ENKSTLHPGN
SKLVPYLKST EPAVEKMETD SEDYCVICRF FINGEQFFLQ GRIPRDGTCV LSALHFGDSV
DVTKKLDKLL CCSRCHVRVH ARCYRCTDLS DDSDLAGWLC DVCKYQKEKV VCNLCGTSDS
ALLEYKKNKF CHVQCALLSQ NVRFVCPSLH GGKKMIFQKG PLRGRCDYCD ENKGTLIRCS
EENCNAIFHL HCGRRLGVKY EVADFLTNSK GIHITCEAHS TKFESYVNRR VIVEMSHDHK
EMGYVEDEYE SILYLVDFED GCYSDVLDDD IVSCDCPNRN EKDHIHGVGA RVVLNWIDGK
SYRVILRKAS NEMCYSVMLE KTNSVIHVTR SDFTLAPE
//
