ID A0A0F8VN93_9EURO Unreviewed; 1450 AA.
AC A0A0F8VN93;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-OCT-2025, entry version 33.
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=ARAM_007125 {ECO:0000313|EMBL:KKK24596.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK24596.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK24596.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK24596.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-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:KKK24596.1}.
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; JZBS01000966; KKK24596.1; -; Genomic_DNA.
DR STRING; 308745.A0A0F8VN93; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000034291; 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 FunFam; 2.60.120.650:FF:000047; 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:UP000034291};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 80..121
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 350..513
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 594..719
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..59
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..985
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1076
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1450 AA; 161787 MW; 6752DD5DC3B7E09B CRC64;
MAAMLDRPPF ESIAAAPATD AASITPPHSI NGMKETPDGV PSELSDLELD ANAAAAQEAP
SIEGEEEEIE PDHYYGGGKV PVFKPTMDQF RDFQAFINRI DKYGMRSGIV KVIPPREWSD
SLPQLDEAIK KIRVKNPIMQ EFHGSHGTYT QANIERQRSY NLPQWKALGE ESSHQPPARR
GERRRNQERA PRAPPAPKPQ TARSDTPKRG PGRPPKRSNQ AKIKEEPIKI KEEPTEESLE
RTKPEGPPTP VSPESNPVET KSEELSDGES LPPPKPRGRQ PKSVTARRKQ NKGDTIDYVD
EEAFKDFDYR IHDSEEYTYE RCEELETAYW KSLMFNNPMY GADMPGSLFD DRTTSWNVAK
LPNLLDVIGQ KVPGVNTAYL YLGMWKATFA WHLEDVDLYS INYIHFGAPK QWYSISQEDA
PRFEQAMKSI WPSDAKNCDQ FLRHKTYLVS PNLLKSQYGI TVNKMVHYEG EFVITYPYGY
HSGYNLGYNC AESVNFATEK WLDYGRVAKK CNCEADSVWI DVEDIDRKLR GESTPEYYGD
FESDLDGLEG ASDLLTPPRS VPEKTSNRGR KRKLDGGDTI KTKRMRVSVD IPRKNLCVLC
PNNLDYEDLL PTEDGKTHAH RRCALYTEET SVLRDESGKE VVCDVDKIPK ARMGLKCLFC
REVRGACFQC NFGKCTRSYH ATCALLAGVQ VEQGLVAVVA DDGNQYSVPS VDLKCKYHRQ
KKPTWLASTE SPEYDRKLIE AARRLVIGDL VQFQADKEIN GAVVLQNRPE ERTLLVKVLP
RGDVIELPYR WMLVVRRSNF FPLAAGIKPL PAHLARKPEA RREVESAMPV AGNPFGDGRS
PYQWAEFETV DSTRHPTAPP AVQVNLDKGE QIWYYLGQSS TECRAQYTHN PSMPVHNPRS
NFLDSVKSLG AVMARLPSSY PHHRLPPFVV AGSAAPPPPP HHFSSAAANT TASAIAVTAA
AAAAAAAASR PSLPQRPPFA PPPRSSPVAT SAAAVAASAM PSAYRSVPTQ SARHAPYPQI
TKSHTSYQQH NHHQQQQQNT SSSHNNNNNI IVNNNNNNNS SSNHTTATTT TASHNHLPAN
NFANVRELIA RRRLAQITDH ANVFAGYTLV GPELVVETLL GPMGSVPPSN GLEKLELAMA
QQRVQPRAPD GTLLPMQPLN MRSEEVTRLL QMLRFSLISH RDRLDVLQKK ESENVKQEMA
NKSTAATPKL PRKYAFLEQQ REQAPSVYQS PYDMPSGFTE YARTTFGLTR HEPELPKPSL
ANDYFASLSP EDQEKILKTC GSFVQRAMER SVTHSRQSSS ASNLRLASAL AQQTENPTID
ITTVEDLPLS GLDFPLHADS PCSNFSRSHL RFQSPNDFTS HGVEVHHDHH DLFGDQQANT
RFWQHGPWAV GDGNTPNEES RPFFGPHERL KHDYASSDIS LGRGPGSLHS VDMAGFGLDN
PDDLCTVLSP
//
