ID A0A1E1JRX1_9HELO Unreviewed; 1507 AA.
AC A0A1E1JRX1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-OCT-2025, entry version 28.
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=RCO7_04444 {ECO:0000313|EMBL:CZS88635.1};
OS Rhynchosporium graminicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Ploettnerulaceae; Rhynchosporium.
OX NCBI_TaxID=2792576 {ECO:0000313|EMBL:CZS88635.1, ECO:0000313|Proteomes:UP000178129};
RN [1] {ECO:0000313|Proteomes:UP000178129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UK7 {ECO:0000313|Proteomes:UP000178129};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 2-
CC oxoglutarate + 2 O2 = N(6)-methyl-L-lysyl(9)-[histone H3] + 2
CC formaldehyde + 2 succinate + 2 CO2; 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:ARBA00049349};
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CZS88635.1}.
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DR EMBL; FJUW01000002; CZS88635.1; -; Genomic_DNA.
DR STRING; 914237.A0A1E1JRX1; -.
DR InParanoid; A0A1E1JRX1; -.
DR Proteomes; UP000178129; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0051864; F:histone H3K36 demethylase activity; IEA:TreeGrafter.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR CDD; cd15571; ePHD; 1.
DR FunFam; 2.60.120.650:FF:000024; Putative jumonji family transcription factor; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR055500; DUF7072.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694:SF7; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF23258; DUF7072; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000178129};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 62..103
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 323..486
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 576..705
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..189
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..202
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..525
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1005
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1041
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1086
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1170
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1290
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1507 AA; 167650 MW; FB0B160BF876F551 CRC64;
MSADTMAVPA AQDTSVGLNS PPDSNSALKD GGSDSELSDL EPDIDINEKL EIEPDHISSG
GVPVFKPTME EFVDFTRYMG AVNKYGMRTG IVKVIPPAEW VAAQPRLDEA IKTVRVKEPI
KQDIMGTGGT YRQANIVHQR SYNLPQWRQL CEQSEHQPPA KRGERRAAPE KTTKSTPKSK
TAGPSSTSGA KKRPGRPPKN KPRSATVEQD GTSTPDRLPT PVSPTMKPED DNDSVKLEQE
DYDMPNKVRG GRQPKAISVS SRRKNNKRET GVVDEAAFQD FKYELEGEDY SQERCEELER
NYWKTLTYAP PLYGADMPGT LFDERTTSWN LGKLDNILDV LGSKIPGVNT AYLYLGMWKA
TFAWHLEDVD LYSINYLHFG APKQWYSISQ GDARRFEAAM KTIWPTDAKA CDQFLRHKTF
LISPSQLLSN YNIKVNKIVH HPGEFVITFP YGYHSGYNLG YNCAEAVNFG LESWLEYGRV
AKKCECSEAQ DSVWIDVHEI DRKLRGEETE DEETDDEEDE EEDEEGSKST ILLTAPEASG
NVKPKLVKKK RKRPTNEKVE NSNVKRIRMR IKAPTREPCI LCPNDIPSEP LLLTEDGEKA
HRMCAQYIPE TSILAGEKET IVDVKYIDKA RLDLKCNYCR SRKGACFQCS QKKCTRAYHA
TCAAAAGVLV EQGETPVFGE DGTEYKDWGI DFSCRFHRSK RDKKADGDSL GEDKRLLKAG
LDLKAGDVCQ MQYFKGDIFA GTVVENRSSE EMILVDILPR GHVSDMEHML PRLTCYSDRV
EVEYKWLLVP DLAERRLQKP SSKAIPMPKS FKAKESLNTS KRQADDLPRA EDPFVEGCTW
AEFKCEPIRH NPAQVRIDFS KEDQIWFYLG KNSTEAKAQF TEDPTKPRHN PKGHFLDTIP
KPAPAVQRQS YSASHPTNFN SNPPSFSKAP IRPPQPVTSS IKPEKPYVYK PRVGGEMYSV
DQKAYNDQQK FLQRSAPAPY AFGTDPQYRQ PDPPRPPAQY APILPPGSNS GARPVSQMAA
PRPASSLATA RSSASTPRSS PAMPPPRYGP SMPASYPSYR PPVPPAQRPM NPFGSRPPSS
SSKPNPFAKY SYLQKEHNRS PLEYKSPYRP GGGFMNGYQG SLQAHLQQTL FRNNSGQPST
PMSSISSFGS SLRPYSSSSQ SPVSSYKPNS PAAYNTYRTS ATPTPAPVSS PAPQQHRATV
PPEKDSVQLH PAIRQEYNSV VPQKYPTTAP SSSSQFNGSV LQPPAMYDRI ATQLQAPYQT
FSTPQQARYR THHELQAPLT QQAPQQSHQN CPPPPPSPHN GYHPVSAHQN PRLPVSHTQY
HSHSAPMSAV SPAYSPISQT QGKPPQRSPD QALVSQQTPQ PPTAAWKPSP HASFAQQYSP
APVAATPASI VPQHSPAPMP THTSAKPPVS QDNYRSHPAM PVPAPYRSDV YYQSQPPPPL
RAPTQDGKVL YPHQPYYQPS NSQNTDQQAG ASAPNQNPQR RAFPDVPADS TTLVEKMMMA
LKRAPAT
//
