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Database: UniProt
Entry: A0A7U2N1A1_ASPFN
LinkDB: A0A7U2N1A1_ASPFN
Original site: A0A7U2N1A1_ASPFN 
ID   A0A7U2N1A1_ASPFN        Unreviewed;      1395 AA.
AC   A0A7U2N1A1;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 7.
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=F9C07_2167825 {ECO:0000313|EMBL:QRD93679.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:QRD93679.1, ECO:0000313|Proteomes:UP000596276};
RN   [1] {ECO:0000313|Proteomes:UP000596276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167 {ECO:0000313|Proteomes:UP000596276};
RX   PubMed=34849826; DOI=10.1093/g3journal/jkab213;
RA   Skerker J.M., Pianalto K.M., Mondo S.J., Yang K., Arkin A.P., Keller N.P.,
RA   Grigoriev I.V., Louise Glass N.L.;
RT   "Chromosome assembled and annotated genome sequence of Aspergillus flavus
RT   NRRL 3357.";
RL   G3 (Bethesda) 11:jkab213-jkab213(2021).
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}.
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DR   EMBL; CP044623; QRD93679.1; -; Genomic_DNA.
DR   Proteomes; UP000596276; Chromosome 6.
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:UP000596276};
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..53
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..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          918..1021
FT                   /note="Disordered"
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        922..944
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        961..975
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1000..1018
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1395 AA;  156211 MW;  4BDEEDEE6EEDDC81 CRC64;
     MMATALDQPL FESVAGPATA AASITPPHSA NGKKEVPDGV PSELSDLELD PNAVGVPEAA
     SVEEEEEDIE PDHYYGGGKI PVFKPTMDQF RDFQSFINKV EKYGMRSGIL KVIPPKEWTD
     SLPALDEAVK KIRVKNPIMQ EFHGSHGTYT QANIERQRSY NLPQWKGLCE ESSHQPPARR
     GERRRNQERI TRAPPSSRAQ TARPDSQKRR PGPGRPPKRS NQVKVKEEPA EDTLDKIKPE
     GPPTPVSPES NPVEAKTEEL SDGESLPAPK PKGRQPKSVT SRRKHNKGDA IDYVDEEAFK
     DFDYRIHDNE EYTQERCEEL ETAYWKSLMF NNPLYGADMP GSLFDENITT SWNVARLPNL
     LDVLGQKVPG VNTAYLYLGM WKATFAWHLE DVDLYSINYI HFGAPKQWYS ISQEDAPKFE
     QAMKSIWPSD AKNCDQFLRH KTYLVSPSLL KSQYGITVNR LVHYEGEFVI TYPYGYHSGY
     NLGYNCAESV NFATEKWLDY GRVAKKCHCE SDSVWIDVDE IERKLRGEAT PEYYPEFESD
     LDEFEGASDL LTPPRSVPEK SNRGRKRKHD GDTTKAKRMR 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 YATAPPHHLS PAAAAAATAA AAASRPSLLQ RPTLAPPPRT
     PSSAAPPAST AMPSAYRSLP TQSARHAPYP QIAKTHQSHH LSQQQHSPQQ SQQQQQQQHS
     HHLPANTFAN VRELIARRRL AQITDHANVF AGYTIVSPEL VVETLLGPMG SVPPPTGLEK
     LELAMAQQRV QPRAADGTLL PLQPLNMRSE EVTRLLQMLR FSLVSHRDRL DVLQKKETEN
     NKQESAHKGS VAAVKLPRKF AYLEQQQEQS PTVYQSPYNM PSGFSEYAQK TFGLTPSEPE
     LPKPSLANDY FASLSPEDQE KILKTCGSFV QRAIERSASH SRQSSASNLR LASALAQQTE
     NPTIDITTVE DMPLSGLDFP LHADSPCSSF SRPHLRFQSP NDYNAHGPET HHDHHDLFGD
     QQANTRFWQH GPWAAGDGNT PNEETRPFFG PHERLKHDYA SSDISLGRGP GSLHSVDMAG
     FGMDATDDLC NVLSP
//
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