ID A0A8H6UHR6_9EURO Unreviewed; 1422 AA.
AC A0A8H6UHR6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 14.
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=CNMCM5793_002988 {ECO:0000313|EMBL:KAF7113632.1},
GN CNMCM6106_002733 {ECO:0000313|EMBL:KAF7155278.1};
OS Aspergillus hiratsukae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=1194566 {ECO:0000313|EMBL:KAF7155278.1, ECO:0000313|Proteomes:UP000662466};
RN [1] {ECO:0000313|EMBL:KAF7155278.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM5793 {ECO:0000313|EMBL:KAF7113632.1}, and CNM-CM6106
RC {ECO:0000313|EMBL:KAF7155278.1};
RA Dos Santos R.A.C., Rivero-Menendez O., Steenwyk J.L., Mead M.E.,
RA Goldman G.H., Alastruey-Izquierdo A., Rokas A.;
RT "Draft genome sequences of strains closely related to Aspergillus parafelis
RT and Aspergillus hiratsukae.";
RL Submitted (JUN-2020) 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:KAF7155278.1}.
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DR EMBL; JACBAD010002130; KAF7113632.1; -; Genomic_DNA.
DR EMBL; JACBAF010002320; KAF7155278.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000630445; Unassembled WGS sequence.
DR Proteomes; UP000662466; 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:UP000630445};
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 345..508
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 589..714
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..292
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 948..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..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 948..957
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..967
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..978
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1052
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1422 AA; 157971 MW; E5F3C8D1D3A76595 CRC64;
MMAAALDQPP FDSLAGSRPN DAVSITPPHS ANGKKEAPDG VPSELSDLEL DPGTSAVKIE
DSVEGEEDVI EPDHYYGGGK IPVFKPTMAQ FRDFQAFINK VDSYGMRSGI VKVIPPKEWL
DAQPPLDEAV KKIRVKNPIM QEFHGSHGTY TQANIERQRT YNLPQWKALC EESSHQPPAR
RGERRRNQER ATRTPAAPKI QTARSSSQKR GPGRPPKRVN QVKVKEEPPA DEVLEKTKPE
GPPTPVSPES NPVETKSEEL SDGESLPGPK PKGRQPKSVT ARRKHNKGDN VDLVDEEAFK
NFDYRIHDQE EYTQERCEEL ETAYWKSLMF NNPLYGADMP GSLFDDSTTS WNVAKLPNLL
DVIGQKVPGV NTAYLYLGMW KATFAWHLED VDLYSINYIH FGAPKQWYSI SQEDAPRFEQ
VMKSIWPSDA KSCDQFLRHK TYLVSPSLLK SQYGITVNRL VHYEGEFVIT YPYGYHSGFN
LGYNCAESVN FATEKWLDYG RVAKKCNCEA DSVWIDVDEI ERKLRGEATP EYYDEFDSDM
DVMMDGASDL LTPPRSVPEK TSNRGRKRKH PGETTKAKRM RVNVEIPRKA PCVLCPNDLD
YEDLLPTEDG KSHAHRRCAL YTEETSILRD ESGKEVVCDI DYIPKARMGL KCLFCREVRG
ACFQCNFGKC TRSYHATCAL LAGVQVEHGS IAVIADDGNQ YSVPSVDLKC KYHRQKRPTW
MTNDAADYNR KLNATAQRLV AGDLVQFQAD KEINGAVVLQ NRPEERTLLV KILPRGWLLI
VRKSNFTPLV PGTKPLPAHL ARKPDARKEL ESAVPVAGNP FGDGRSPYQW AEFETVDVTK
HVSAPPPLHV DLDKGEQMWY YMGQSSTECR AQYTHNPSVS VHNPRSNFLD SVKSLGGVVT
RIPSYPHHFP QYASAAVGAP PRNHHLLSPA TATAAAAAAA SAAAAAAANR PSLLQRPPLA
PPPPPAAPRS SSSTVASAAA ASAMPSAYRT LPSQSARHAP YPQVIKAHHH HHHHQQQQQQ
HSFYQPPQAL QTQQQQQNNS TTNNNANNGL PANTFANVRE LIARRRLAQI TDHANVFAGY
TIVSPELVVE TLLGPMGSVP PPNGLEKLEL AMAQQRVQPR APDGTLLPLQ PLNMRSEEVT
RLLQMLRFSL VSHRERLDVL QKQESENIKQ EATARGSAAS AKLAGKYAYL DQQRAQAPTV
YQSPYDMPSG FTEYAKKTYG LIPCAPELPK PSLANDYFAS LSTEDQEKIL KTCGSFVQRA
IERSATHSRQ NSGSNLRLAS ALAQQTENPT IDITTVEDLP LSGLDLPLHA DSPCSSFSRS
HLRFQSPNDF TSHGPEAHHD HHDLFGDQQA NTRFWQHGPW VAGDGNTPNE ENRPFFGPHE
RLKHDYASSD ISLGRGPGSL HSVDMAGFGL DGADDLCAEL SP
//
