ID A0A0M3K5D3_ANISI Unreviewed; 832 AA.
AC A0A0M3K5D3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ORFNames=ASIM_LOCUS15581 {ECO:0000313|EMBL:VDK55562.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001617401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001617401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK55562.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UYRR01032421; VDK55562.1; -; Genomic_DNA.
DR WBParaSite; ASIM_0001617401-mRNA-1; ASIM_0001617401-mRNA-1; ASIM_0001617401.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; 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 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; 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:SF129; LYSINE-SPECIFIC DEMETHYLASE 4A-RELATED; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000267096};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 23..67
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 155..320
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 560..694
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 359..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 832 AA; 95599 MW; D90F513133E62877 CRC64;
MEVASTSGIP GHPTFTSTGT IQVPVFHPTL NEMLDFPGYL NKIEREHGTH LICGIAKIVP
PIGYRMRKCG DYSDVDNYII EQPVKEKVQG HAGIYCKTNK LYRRSMTVKE FRILANKMRF
PKGKLPPEDV EKHYWKTILQ GEPIYGADTP GSICDSDLKE FNMNRLGTIL DMLNESGVKI
KGVNTVYLYF GMWKTTFPWH TEDMDLYSIN YVHFGEPKFW YAIATESNNH FERLCAQSFP
NAAKSCKSFM RHKNFIISPQ ILRRNNIHFG TMIQYANEFI ITFPRGYHMG FNMGYNCAES
TNFASDRWID FGKNAMVCAC RPDSVEIDMR PFMKRFRVNE FNEWHQYWYG ERIVRDNKKR
SAGTSKRQPI HEDNIADIEP TKKQRRGSEK NGGIRGPFID DVHNGDAKVV SINDIVQSTT
NDLGTSIESI ATNKWKKEMR DLWSYLPVNL YAEKEFNNRR ASEAPHCAIC QYFVPKPLME
KRNTLPATSR RIVKRYHYAK MNPDLYDIKE SADLEDRLLR CSNCYVVVHE GCYPVGHIPA
DKSHWRCVRC RRRDDLAVRS TCCHLCELRG GALIPAENAG GDFVHVVCAL LNRRTIFPNP
MTLESAYTRP PMKLNAPIKY ADRPDSQYLS AFGVTQERGK FQCEYCKNTR EGGLLKCYVC
EETLFHATCA RMAGASFEFR NWPDLTVVVC PDHNEVVDDS PALSIGDKVR VYLPEQCSNR
LSKGIVKAVK MQEYCTVNFM DRNWSDDMQP EDIIECECSR INCNGWHIPG AKIKIKWDDG
TVYEGVFRNR YTSSLVSVEL VKPHQHSSNL VELVNVKRDA VFARGERLAD IS
//