ID A0A2G7G1E8_9EURO Unreviewed; 1395 AA.
AC A0A2G7G1E8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-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=AARAC_005398 {ECO:0000313|EMBL:PIG86664.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG86664.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG86664.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG86664.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-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:PIG86664.1}.
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DR EMBL; NEXV01000241; PIG86664.1; -; Genomic_DNA.
DR STRING; 656916.A0A2G7G1E8; -.
DR Proteomes; UP000231358; 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:UP000231358};
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 346..509
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 588..713
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 18..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..218
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..977
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1018
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1395 AA; 156118 MW; BB001F615C165ABB CRC64;
MMATALDQPL FESVAGPATA AASITPPHSA NGKKEVPDGV PSELSDLELD PNAAGVPEAA
SVEEEEEDIE PDHYYGGGKI PVFKPTMDQF RDFQSFINKV EKYGMRSGIL KVIPPKEWTD
SLPALDEAVK KIRVKNPIMQ EFHGSHGTYT QANIERQRSY NLPQWKGLCE ESSHQPPARR
GERRRNQERI TRAPPSSRTQ TARSDSQKRR PGPGRPPKRT NQVKVKEEPA EDTLDKIKPE
GPPTPVSPES NPVEAKTEEL SDGESLPAPK PKGRQPKSVT SRRKHNKGDA IDYVDEEAFK
DFDYRIHDHE EYTQERCEEL ETAYWKSLMF NNPMYGADMP GSLFDENITT SWNVARLPNL
LDVLGQKVPG VNTAYLYLGM WKATFAWHLE DVDLYSINYI HFGAPKQWYS ISQEDAPKFE
QAMKSIWPSD AKNCDQFLRH KTYLVSPSLL KSQYGITVNR LVHYEGEFVI TYPYGYHSGY
NLGYNCAESV NFATEKWLDY GRVAKKCHCE SDSVWIDVDE IERKLRGEST PDYYPEFESD
LDEFEGASDL LTPPRSVPEK SNRGRKRKHD GDSTKAKRMR VNVHVPRKIP CVLCPNDLDY
EDLLPTEDGK NHAHRRCALY TEETSILRDE TGKEVVCDID KIPKARMGLK CLFCREVRGA
CFQCNFGKCT RSYHATCALL AGVQVEQGEI AVIADDGIHY SIPSVDLKCK YHRQKKPSWM
TGGDSPDFDR KLIESAQRMV AGDLVQFQAD KEINGAVVLE NRPAERTLLV KVLPRGDVIE
LPYRWMLVVR RSNFSPLAPG TKPLPAHLAR KPEARKELES ALPVVGNPFG DGRSPYQWAE
FETVDTTNHR FAPPPVQVNL DKGDQIWYYL GQSSTECRAQ YTHNPSVPVH NPRSNFLDSV
KSLGAVMARI PSYPHRHLPQ YAAAPPHHLS PAAAAAAATA AAAAASRPSL LQRPTLAPPP
RTPSSAAPPA STAMPSAYRS LPTQSARHAP YPQIAKTHQS HHLSQQQHNP QQSQQQQQHS
HHLPANTFAN VRELIARRRL AQITDHANVF AGYTIVSPEL VVETLLGPMG SVPPPTGLEK
LELAMAQQRV QPRAADGTLL PLQPLNMRSE EVTRLLQMLR FSLVSHRDRL DVLQKKETEN
NKQESAHKGG VAAVKLPRKF AYLEQQREQS PTVYQSPYDM PSGFSEYAQK TFGLTSSEPE
LPKPSLANDY FASLSPEDQE KILKTCGSFV QRAIERSASH SRQSSASNLR LASALAQQTE
NPTIDITTVE DMPLSGLDFP LHADSPCSSF SRPHLRFQSP NDYNAHGPET HHDHHDLFGD
QQANTRFWQH GPWAAGDGNT PNEETRPFFG PHERLKHDYA SSDISLGRGP GSLHSVDMAG
FGMDATDDLC NVLSP
//
