ID A0A3B3S3N6_9TELE Unreviewed; 1028 AA.
AC A0A3B3S3N6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000025352.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000025352.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B3S3N6; -.
DR STRING; 1676925.ENSPKIP00000025352; -.
DR Ensembl; ENSPKIT00000006085.1; ENSPKIP00000025352.1; ENSPKIG00000008257.1.
DR GeneTree; ENSGT00940000154930; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000261540; Unplaced.
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 GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
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; 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:SF51; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 15..57
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 143..309
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 735..848
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 354..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1028 AA; 116014 MW; 99AB68968C3DC6D9 CRC64;
MTSEPGSQNP SSKSIMTFYP TKEEFKNFSR YIAYMEAQGA HKAGLAKIIP PKDWKPRQSY
DDIDDLVIPA PIQQVVTGQS GLFTQYNIQK KPMTVREFRK TANSDKFCSP RYVDFDELER
KYWKNLTFNP PIYGADVNGT LYDPDVTEWN IGHLNTILDM VERESGITIE GVNTPYLYFG
MWKTTFAWHT EDMDLYSINY LHFGEPKSWY SVPPEHGKRL ERLAKGFFPG SSQNCEAFLR
HKMTLISPSI LRKYGIPFEK MTQEAGQFVV TFPYSYHAGF NHGFNCAEST NFATQRWIEY
GKQAILCSCR KDMVKISMDV FVRKFQPERY KQWKAGKDVV SIDHSKPTPE AAEFLGGEGQ
AGGRAQYAGE GGGAEEETKS LSKQRIGTKR HRVCLEVPEE VLQREQGVEH EGKRLRLSPA
AGGQVSQEGM PECGPGYGAE ELCFLQVLPG DCTPAEEECD DGPPRDDPDA LPPLPRTSSH
CSAIAGPSGG PRPSPKPGVA SLLVHKALSP SDALHVHSYA KGDYSMAAVP SREDRAALGM
DSTLSDGEKG ADEAAENKSM KSKRQPLSKL PRLHPLLRDC ISDEELQEQT TEDEEDIQES
EAWAKPLAQL WQNRPQNPKA EKEYNQRMGL QAPYCAICML FQTYQQSEFD CSSQKPPEAD
GKWPRSKPLI PEMCFTSTNT SEVHISTPYM EEDNTSLLVR CSQCSIRVHI SCYGVPREKV
SDDWRCARCE ANALTEDCCL CSLRGGALQR ANNDKWVHVL CAVAVLEARF LNLVERGPVD
LSGIPLQRFK LKCLYCKKRM KRAVGCCVQC SHGRCSTSFH ATCAQAAGVL MQPDDWPFVV
YVTCWRHKGP GHGERNRASL RDLEAGQKVI CKHKNGRYYQ CEIVQQTKAT FYEVIFDDGS
FSDNLFPEDI VNRDCMQLGP PAEGDVVQVR WTDGLVYGAK FVAAHVIPMY QVEFEDASQL
TAKRDDVYTL DEELPKRVQT RLSVASDMRF DGIFTEKEVR RDSKRQRVIN SRYRGDYIEP
VIYRAIME
//
