ID A0A4X2LLW5_VOMUR Unreviewed; 1004 AA.
AC A0A4X2LLW5;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=KDM4A {ECO:0000313|Ensembl:ENSVURP00010024948.1};
OS Vombatus ursinus (Common wombat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Vombatidae; Vombatus.
OX NCBI_TaxID=29139 {ECO:0000313|Ensembl:ENSVURP00010024948.1, ECO:0000313|Proteomes:UP000314987};
RN [1] {ECO:0000313|Proteomes:UP000314987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yazar S.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSVURP00010024948.1}
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; A0A4X2LLW5; -.
DR Ensembl; ENSVURT00010028407.1; ENSVURP00010024948.1; ENSVURG00010019117.1.
DR GeneTree; ENSGT00940000159643; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000314987; Unassembled WGS sequence.
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); 2.
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; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF119; LYSINE-SPECIFIC DEMETHYLASE 4A; 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:UP000314987};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 14..56
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 142..308
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 711..824
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 353..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..477
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1004 AA; 113959 MW; 44AD6D82E5458941 CRC64;
MASESESLNP SARIMTFYPT MEEFRTFSRY IAYIESQGAH RAGLAKVVPP KEWKPRSTYD
DIDDLVIPAP IQQVVTGQSG LFTQYNIQKK AMTVREFRRI ANSDKYCTPR YNEFEELERK
YWKNLTFNPP IYGADVNGTL YEKHVDEWNI GRLNTILDVV ENESGITIEG VNTPYLYFGM
WKTSFAWHTE DMDLYSINYL HFGEPKSWYS IPPEHGKRLE RLAKGFFPGS AQSCEAFLRH
KMTLISPSIL KKYGIPFDKV TQEAGEFMIT FPYGYHAGFN HGFNCAESTN FATLRWIEYG
KQSVLCSCRK DMVKISMDVF VRKFQPERYK LWKAGKDAPV IDHTLPTPEA AEFHKGEQQD
CPEEALDSSG DPGSEAARRS PTRHRIGAKR HRVCLEVPQE VSESEAFAQR EPYEMDGEQT
AVVPGKAVPD LVSPLRAENG TLLSPDYPDC AEVRFEELKN VKLEDEDEDE EEEEAAALDL
SLSSTTNQAS KKSRARSSEA RSHRARQALT AHSCAQDDDS EQELSENEEE ESQKAKGRRQ
PLSKLPRHHP LVAQDCGSDD EAGEQLTPEE EAEETEPWAK PLSQLWQNRP LNFEAERVYN
ESMAQQPPHC AVCMIFQTYQ QAEGGGHNQS WTDADPGRRR TKPLIPEMCF TATGCSTDLS
LSTPYLEEDG TSILITCKKC CVCVHASCYG VSPEQASDDW MCSRCSASAL EEGCCLCSLR
GGALQRANDD RWVHVMCAIA VLEAKFVNIA ERSPVDLSRI PLLRFKLKCV FCKKRRKRVA
GCCVQCSHGR CPTSFHVSCA QAAGVMMQPD DWPFVVFITC FRHKVPSQAE RAKGALQDLS
AGQTVISKHK NGRFYQCEVV QLTTETFYEV NFDDGSFSDN LYPEDIVSRD CLQLGPPAGG
EVVQVRWTDG QVYGATFVAS HPIQMYQVEF EDGSQLMVKR DDVYTLDEEL PKRVKSRLSV
ASDMRFTEIF TEKDVRQEKK RQRVINSRYR EDYIEPALYR AIME
//
