ID A0A0N0U840_9HYME Unreviewed; 1407 AA.
AC A0A0N0U840;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=WN51_10715 {ECO:0000313|EMBL:KOX81382.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX81382.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX81382.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX81382.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX81382.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) 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 -!- 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 EMBL; KQ435687; KOX81382.1; -; Genomic_DNA.
DR STRING; 166423.A0A0N0U840; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000053105; 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 GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 1.
DR CDD; cd15493; PHD_JMJD2; 1.
DR CDD; cd20391; Tudor_JMJD2_rpt1; 1.
DR CDD; cd20392; Tudor_JMJD2_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; 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:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 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 Methyltransferase {ECO:0000313|EMBL:KOX81382.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Transferase {ECO:0000313|EMBL:KOX81382.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 12..54
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 142..308
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1141..1249
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 457..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..574
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1407 AA; 158847 MW; F2B11900054259C2 CRC64;
MVSNISRGTP RIQVFRPTYE EFMDFTKYVE YMESKGAHKA GLAKVIPPPE WIPRKKGYDL
DDLDLTIPAP ICQVVTGKQG LYQQINIQKK SMTVKEYSKM ANSERYNTPR HFDYEDLERK
YWKNITYVAP IYGADVSGSL TDPDVKEWNI NHLGTILDYV NKDYGISIDG VNTAYLYFGM
WKTTFAWHTE DMDLYSINYL HFGAPKTWYA IPPEHGRRLE RLASGFFPSS YQSCQAFLRH
KMSLISPQVL RQYSIPCNKI TQEAGEIMIT FPYGYHAGFN HGFNCAESTN FAAPRWVEYG
KRATQCTCSK DMVKISMDTF VKRFQPERYE LWLRGEDIGP HPEDPKQTAA PMPSQMDLLC
SNSSNGQLPQ SYLNAAPKNK RHTIHKKKNL MATNSDVDME ELVNRSDIPP DVKKVLQDLE
LEEVDDQPDE QQLEVLEDIW LKAGEMDVDE ASVYDDGYNR KKSRKRKRKN TDKDKSKSKK
ECNKSITDGV TIKTEIKMEI DDSFNFLPSA EQSTQLEKVD QRSSNVIMSR ENVVGNIKIE
ENSDFLEVSD KPVKKRKKHS KSGEPKKVKS KNINKTKRKH LDISIFNTNE PLDVSDADVQ
RQLMAMPSLN LHKSTVNKEI ANHLSGTTVF LDNEASVSPV KEKSVINITN SNHVSNSIYS
DAKETEKILD NNADERMNLY AKSTKKSSIA TIKPTFPKQI SLKNISLDQV KPANKIDKAV
ESEYIGEDTN VTIQETKPGT YTSCKSVGTI ISERSILNYP KKDIIKAPRL SVLKSANIVI
SPKTWPIVKP REPKLSTPGV MFLNTNFSNP PILQKEIPQE IGNETKSVEA SKSVTPGAIQ
IPRLEGIFAK NAVLAQPLNQ SVMRVTGTNT DIKTLGKRSS TETSKMIATK FWQSSSGNNS
LFFLKDVRDD KQAHPIVAKV DTSEASLNLT GNNTLFLATT SNPESMCASI PSLKQLTSSR
RKSKEKLKKS ITRKKEPTET KTLATTNSMS NSDEANIVTC SVDQSMSHRV SMIPGHISDM
LYPSVPNNDL LKAFNDYWSA QISHCAICAP FTSSCNGHSR LMPPDWKYCK PTVLPESSPI
WVSANIFVAN SKEQIVEPEN DKLLRCRECH VTVHASCYGI TVLPTDLRNW ACDKCKAGKT
QVMCCLCPMR GGALKRTSDS NWAHILCALL LPGVTFKDAI NKDPINVLTI KPDNVKQQCC
YCGQKDGACL KCNYCTNLFH PSCGLVSGAT FTIPVYNSLE LQVTCDGHDD GKEKIPPLRQ
GEIVWAKHRN TRYYKAKVDS IHDTLFYMVT FSDNSFSDDL YPSDIMNYDP GNPPQQGAAV
VVKWTDGNLY NGIFEGTNHR IMYTVSFEDG SQLPLKRNDI YSLQEDMPKR VRSRLSVATE
MKHRYHLYGM EDESEAQRKV KQSKYCD
//
