ID A0A395GJ93_9EURO Unreviewed; 1427 AA.
AC A0A395GJ93;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 02-APR-2025, entry version 20.
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=BO80DRAFT_368446 {ECO:0000313|EMBL:RAK95555.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAK95555.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAK95555.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAK95555.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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}.
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DR EMBL; KZ824490; RAK95555.1; -; Genomic_DNA.
DR RefSeq; XP_025569883.1; XM_025716336.1.
DR STRING; 1448316.A0A395GJ93; -.
DR GeneID; 37221201; -.
DR VEuPathDB; FungiDB:BO80DRAFT_368446; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000249402; 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:UP000249402};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 81..122
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 347..510
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 590..715
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 15..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1056
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..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1007
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1043
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1427 AA; 158711 MW; F6EF9486D2ACBD69 CRC64;
MMAAALDQPL FESIAGGPAT DAASITPPQS VTGKKEVPDG VPSELSDLEL DPNATGAQEI
PSVEADDEEI EPDHYYGGGK IPVFKPTMDQ FRDFQSFINK VEEYGMRSGI IKVIPPKEWT
DSLPALDEAV KKIRVKNPIM QEFHGSHGTY TQANIERQRS YNLPQWKALC EESSHQPPAR
RGERRKNQER VNRPPAPKAQ TARSDSQKRR PGPGRPPKRA NQVKIKEEPS ADEGLDKIKP
EGPPTPVSPE SNPVEAKTEE LSDGESLPGP KPKGRQPKSV TSRRKHNKGD AIDYVDEEAF
RDFDYRIHDN EDYTYERCEE LETNYWKSLM FNNPLYGADM PGSLFDDNIT TSWNVARLPN
LLDVLGQKVP GVNTAYLYLG MWKATFAWHL EDVDLYSINY IHFGAPKQWY SISQEDAPRF
EQAMKSIWPS DAKNCDQFLR HKTYLVSPNL LKSQYGITVN KLVHYEGEFV ITYPYGYHSG
YNLGYNCAES VNFATEKWLD YGRVAKKCHC EADSVWIDVD EIERKLRGEA TPEYYGEFES
DLDEMEGVSD LLTPPRSVPE KTSTRVRKRK HDGETTKAKR LRVNMEVPRK IPCVLCPNNL
DYEDLLPTED GKSHAHRRCA LYTEETSVLR DESGKEVVCD VDKIPKARMG LKCLFCREVR
GACFQCNFGK CTRSYHATCA LLAGVQVEQG LIAVIADDGN QYSIPSVDLK CKYHRQKKPS
WMASGESPDY DRKLIQTAQG LVAGDLVQFQ ADKEINGAIV LQNRPEERTL LVKVLPRGDV
IELPYRWMLV VRRSNFSPLA PGTRPLPAHL ARKPEARKEL ESAVPVAGNP FGDGRSPYQW
AEFETVDSTN HPNHQAAPPP TQVDLSKGEQ IWYYLGESST ECRAQYTHSP SVPVHNPRSN
FLDSVKSLGA VMARLPSYPH HLAPPHHYAA PHHPHHLSPL TASASAAAVA AVAAAAAAAT
ATAAPSTTTT TAAAAAAASR PSLLQHAPPA PPRPAPSAAV PAAMPSAYRS LPTQSARHAP
YPQVTKSHHS QSHSRPQPLH HHQQQQQQQR SSNLPANNFA NVRELIGRRR LAQITEHANV
FAGYTIVSPE VVVETLLGPL GSVPPPAGLE KLELAMAQQR VQPRAPDGTL LPLQPLNMRS
EEVSRLLQML RFSLVSHRDQ LDVLHKKESE TIKQEPTNGT SLAATKLPRK YAYLEQQREQ
APTVYQSPYD MPSGFTEYAQ KTLGLTPCEP ELPKPSLAND FFASLSPEDQ EKILKTCGSF
VQRAIERSTS HSRQSSASNL RLASALAQQT ENPTIDITTV EDMHFTNLDF PLHADSPCSS
FSRSHLRFQS PNDFANHGPE PHHDHHDLFG DQQANTRFWQ HGPWAAGDGN TPNEETRPFF
GPHERLKHDY ASSDISLGRG GPGSLHSVDM AGFGMDGTDD ICAVLSP
//
