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Database: UniProt
Entry: A0A0M3K5D3_ANISI
LinkDB: A0A0M3K5D3_ANISI
Original site: A0A0M3K5D3_ANISI 
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
//
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