ID A0A1J9QQY2_9EURO Unreviewed; 1546 AA.
AC A0A1J9QQY2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 02-APR-2025, entry version 27.
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=AJ78_01660 {ECO:0000313|EMBL:OJD18284.1};
OS Emergomyces pasteurianus Ep9510.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD18284.1, ECO:0000313|Proteomes:UP000182235};
RN [1] {ECO:0000313|EMBL:OJD18284.1, ECO:0000313|Proteomes:UP000182235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD18284.1,
RC ECO:0000313|Proteomes:UP000182235};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA McEwen J.G.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) 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:OJD18284.1}.
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 EMBL; LGRN01000039; OJD18284.1; -; Genomic_DNA.
DR STRING; 1447872.A0A1J9QQY2; -.
DR VEuPathDB; FungiDB:AJ78_01660; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000182235; 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:UP000182235};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 129..170
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 390..553
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 635..760
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..105
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..329
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1477
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1546 AA; 171075 MW; F2533B9CBBEED54D CRC64;
MAAESSAEAI VTMSPRADKL DDINNNKTDN TTASMTPPAS ADGEKISSSS IDNNNTSSSS
AASSASSSPS ELSDIDLDSN TNTNTNTNTN SNSNSNSTST SNTTTAPDQT STTASGEIHP
DHYYGGGKIP VFKPTMDQFR DFAAFVQKVD SYGMKSGVIK IIPPKEWTDA LPSLDEPIKT
IRVKNPIMQE FHGSHGMFTQ ANIEKQRSYN LPQWKSLCEE SSHQPPARRG ERRRNQERVN
RGAAHKPSSR SGSQRRKPGP KPKRVEVDKP MEDSSENHVD KSKPESPPTP VSPESKPVET
KTEVLSDGES LPAPKPKGRQ PKSVSARRKY NRGDAADYID EEAFKDFDYR LSGTEEFTPE
RCEELETAYW KSLMYNNPMY GADMPGSLFD DSVTSWNVAK LPNLLDVLGQ KVPGVNTAYL
YLGMWKATFA WHLEDVDLYS INYIHFGAPK QWYSISQEDM GKFEAAMKSI WPTDAKNCDQ
FLRHKTYLIS PSLLKSQFGI SVNKMVHYEG EFVITYPYGY HSGFNLGYNC AESVNFATES
WLDYARVAKK CNCEADSVWI DIGEIERKLR GESTPEYYDE MGSDQDEMDM DGVSDLLTPP
RSVPEKSGTR VRKRKREGQE SKTKRSKLHV GGPKKVRCVL CPNTMDYEEL LATEDGKSHA
HRRCATYIEE TTILKDDSGT EVVCDIDKVP KARLGLKCLF CREINGACFQ CMHGKCTRAY
HPTCALLAGV QVEFGAIAVM ADDGYEYSVP GVDLKCKYHR PKKYAYMQGE TLDLDPKLAQ
TARNIRVGEL VQFQADKEIN GAVVLENRPT ERSMLVKVLP RGDVIELPYR FLLVVKKSSF
PPLPAGIKPL PSHLARKPDA KKDLASSLPS PGTPFGDARF VYQWGEFISA KPPYNSSSTK
VDLSKPEQIW YYLGNSSTEC RAQYTENPNR SSHNPRSHFL ESVKSLNAPV VTTHHPHHPH
HPSYARNYPS SPFARHQTVP QRPTVTSVSV PQPTQTAIAK LQPVKSTTVG NAITSATTGT
ATNITHNLKS QPVKSSQITF QLPTSQPANP QLPIEKPQLQ EPYDNNHKMS VWAGDITSQF
TMARRLVASI TDHANLRAGY TIVDSDFVVQ TLLGQAGSVL PKNGMEKLKT AMSESMVKPK
SSDHNKNNKT KNNDADCGPL QPLNMKADEV DHLLRMLRFA LMNLTPKGAT TVEKKPPEEK
APQEVPVKEP CGPRPKIEGR YAYLDMQRRQ LATIYQSPYA PGFGFSDYAR REYNLIVEVF
AEPKPSLAIE YFEGLSREDK DKVIEACGLD VTVPRRKMRM QIPTVEEHLA LDAGSNHNPV
VGVGVSRFGQ QPLSLSSSSS FPGPSSLDAM TIDDPHNHHH QNNNIHNQNQ HHLSVFDMHM
SMTMSLPASA DSPASASGCS TFGRPPLRYQ SPHDFSLHIE HESSILPRHL QLHDHDLFGD
QQANQRFWQR SVVPWVDGDC GNSDAGGGSG AAGGGSGDVK SQDGRDRDEH RPFFGPHERP
PGVGGGGSMG NDYASSDLDM GRGPGSLHSM DMVGFGFDGP EEDGSP
//
