ID A0A671UDR3_SPAAU Unreviewed; 909 AA.
AC A0A671UDR3;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
OS Sparus aurata (Gilthead sea bream).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Sparus.
OX NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010012471.1, ECO:0000313|Proteomes:UP000472265};
RN [1] {ECO:0000313|Ensembl:ENSSAUP00010012471.1}
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 -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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DR AlphaFoldDB; A0A671UDR3; -.
DR Ensembl; ENSSAUT00010013256.1; ENSSAUP00010012471.1; ENSSAUG00010001675.1.
DR GeneTree; ENSGT00940000159248; -.
DR Proteomes; UP000472265; Unplaced.
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; 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; 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:SF30; LYSINE-SPECIFIC DEMETHYLASE 4B; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF18104; Tudor_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 SUPFAM; SSF63748; Tudor/PWWP/MBT; 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:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000472265};
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 670..784
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 401..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 103285 MW; 33FDD98990BF464A CRC64;
AGQKGRGANP SCKIMTFRPT MEEFKDFAKY IVYMESQGAH RAGLAKVIPP EGWKPRRSYD
TIEDMVIPAP IMQVVTGQSG LFTQYNIQKK SMTVSEYRKL ANSKRYCTPR HKDFDDLERK
YWKNLTFVSP IYGADVSGSI YDEDIHEWNI GHLNTLLDMV EQECGIVIEG VNTPYLYFGM
WKTTFAWHTE DMDLYSINYL HFGQSKSWYA IPPEHGKRLE RLAQGFFPGS SQGCDAFLRH
KMTLISPSIL KMYGIPFDRI TQNEGEFMIT FPYGYHAGFN HGFNCAESTN FATLRWVDYG
KMATQCTCRK DMVKISMDVF VRCLQPDRYE LWKQGKDTAV LDHLKATELS SPELESWRQQ
RITHRANLLR SCFILNFTRS FLSSCCWFMK YEKLNLTRNI PHSKRHLPPQ KPEAKPQNLM
EDIEKKKPKK PKKTTNTSIT GFEEAFEQFA TSNIKTSNNV SFAAEVAKPL IPKQSDIPAD
NKLDVSATQA CFSKMKMPTE VKKSRRHPLS KPPKRSPLSI LKQDPTSEKE LSSPMPLESD
MKKQEHLWQN QSPNFLAEKA FNAAVAALQP HCAICSLFCP YAKVQPQTTA HTSLFHPTRT
RPLVPEMCFS VGARNTEPPP TNYHIAEDGT SVLLCCSSCH MQVHSSCYGV KPESITEPWM
CSRCVAGAWT VECCLCNLRG GALKTTTDKR WVHVICAIAV AEARFVNTIE REPVDVSAVP
ESRKNLKCVF CHSKNANQNR GACIQCSSEK CATSFHVTCA QIAGVVMTPA DWPYVVTVTC
HKHKRVPPKV RSIRILVLVI GRNIDSWYYH CTIVGMATQT FYEVNFDDGS YCDNVHPENI
LVSVFTSHDC LHSGPPDVGE LIMVSMPEGQ LLNASFVRQH TLQFYQVRKN PNIRWQPQSV
QAKPSELCD
//
