ID A0A3A3A0Y6_9EURO Unreviewed; 1354 AA.
AC A0A3A3A0Y6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 02-APR-2025, entry version 22.
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=PHISCL_04672 {ECO:0000313|EMBL:RJE22981.1};
OS Aspergillus sclerotialis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Polypaecilum.
OX NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE22981.1, ECO:0000313|Proteomes:UP000266188};
RN [1] {ECO:0000313|Proteomes:UP000266188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA Tafer H., Lopandic K.;
RL Submitted (FEB-2017) 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:RJE22981.1}.
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DR EMBL; MVGC01000141; RJE22981.1; -; Genomic_DNA.
DR STRING; 2070753.A0A3A3A0Y6; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000266188; 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:UP000266188};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 77..118
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 344..507
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 587..712
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..284
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..939
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..960
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1354 AA; 151803 MW; 6B0C9A1AFF28D9AE CRC64;
MAAVLDQSRF ESLANPPPPE GASITPPHST NGKGDGSEGA PSELSDMDID PKPAAQPDAA
ADEEEIEPDH FYGGGRIPVF KPTMDQFRDF QSFINRVDKY GMQSGIIKVI PPKEWSDALP
ALDEAVKKIR VKNPIMQEFH GSHGTYTQAN IERQRSYNLP QWKGLCEESS HQPPARRGER
RRNQRNQERA TRAAPTPKPQ ATRSDSQKRG PGRPPKRSNQ VKIKEEPPAD EGLEKTKPEG
PPTPVSPESN PVETKSEDLS DGESLPAKPK GRQPKSVTAR RKHNKGDTVD WVDEEAFKGF
DYRIHDNSEY TQERCEELET AYWKSLMFNN PMYGADMPGS LFDEDITTSW NVAKLPNLLD
VIGQKVPGVN TAYLYLGMWK ATFAWHLEDV DLYSINYIHF GAPKQWYSIS QEDAPRFEQA
MRSIWPSDAK NCDQFLRHKT YLVSPSLLKS QYGITVNKMV HYEGEFVITY PYGYHSGYNL
GYNCAESVNF ATEKWLDYGR IAKKCNCEAD SVWIDVDEIE RKLRGESTPE YYGEYESDLD
EMEGVSDLLT PPRSVPEKTS TRGRKRKLDG AVPKGKRAKV HVEIPRKLPC LLCPNDLDYE
DLLPTEDGKS QAHRRCASFI EETSILRNES GQEVVCDIDK IPKARMGLKC LFCREVRGAC
FQCNFGKCTR AYHATCALLA GVQVEQGLVA VIADDGNQYS IPSVDLKCKY HRQKKNTWIA
SEPSQYDRKI NETAQHLGMG DLIQFQADKE INGAIVLQNR PEERTMLVKV LPRGAGVLIG
ANRDVIELPY RWMLVVRKSN FTPLVPGTKP LPAHLARKPD QRKELESAIP VAGNPFTDGT
SPYQWAEFEM VDNFAPPVHV NLDKEEQIWY YMGQTSTECR AQYTHNPTVP IHNPRANFLD
SVKTLGGNRH SSSYYPHRIP HHAPPPHLLP PSSRHSLQHP YPPPPPSSAP AAAAASAMPS
AYRSLPSQSV RHAPYPQIAK SRQQHIPPNT FANVRELIAR RRLAQITDHA NIFAGYTIVS
PELVVETLLG PMGSVPPPSG LEKLELAMAQ QRVQPRAADG TLLPMQPLNM RSEEVTRLLQ
MLRFSIVSHR ERLDVLQKKE SENVKPVDRN SIAAAKLSGK YAYLDQQRSQ APAVYQSPYD
TLGFSQHAKE TFELAPCEPE LPKPSLANDF FASLSQEDQE KVMKTCGSYV QRQIERSASH
SRHSSASNLR LSSALAQETD NPTIDITTVE DMPLTGLDLP LHADSPCSSF SRSHLRFQSP
NDFTSHPESH HDHQDLFGDQ QANMRFWQHG PWAAGDGNTP NEENRPFFGP HERLKHDYAS
SEISLGRGPG SLHSVDMAGF GLDGTDDLCA ELSP
//
