ID G3YH99_ASPNA Unreviewed; 1373 AA.
AC G3YH99;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=ASPNIDRAFT_52694 {ECO:0000313|EMBL:EHA18096.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA18096.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA18096.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; 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:ARBA00000040};
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:EHA18096.1}.
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DR EMBL; ACJE01000021; EHA18096.1; -; Genomic_DNA.
DR STRING; 380704.G3YH99; -.
DR HOGENOM; CLU_001442_1_3_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 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; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 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 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 76..117
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 343..506
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 586..705
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 15..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..944
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1373 AA; 153002 MW; 24FC961E12375D71 CRC64;
MAAALDQPLF DPIAGAPATD AASITPPQSV NGKKEVPDGV PSELSDLELD PNVNGAKEIP
SVEADDEEIE PDHYYGGGKI PVFKPFRDFQ SFINKVEEYG MRSGIIKVIP PKEWTDSLPP
LDEAVKKIRV KNPIMQEFHG SHGTYTQANI ERQRSYNLPQ WKALCEESSH QPPARRGERR
RNQDRVTRAP SAPKTQATRS DSQKRRAGPG RPPKRANQVK VKEEPPADEG LDKIKPEGPP
TPVSPESNPV EAKNEELSDG ESLPGPKPKG RQPKSVTSRR KHNKGDAIDY VDEEAFQDFD
YRIDDSQDYT YERCEELETN YWKSLMFNNP LYGADMPGSL FDDNITTSWN VARLPNLLDV
LGQKVPGVNT AYLYLGMWKA TFAWHLEDVD LYSINYIHFG APKQWYSISQ EDAPRFEQAM
KSIWQSDAKN CDQFLRHKTY LVSPNLLKSQ YGITVNKLVH YEGEFVITYP YGYHSGYNLG
YNCAESVNFA TEKWLDYGRV AKKCNCEADS VWIDVDEIER KLRGEATPEY FGEYESDLDE
IEGASDLLTP PRSVPEKTST RGRKRKNDGE TTKAKRMRVA MEVPRKIPCV LCPNNLDYED
LLPTEDGKSH AHRRCALYTE ETSILRDESG KEVVCDVDKI PKARMGLKLR GACFQCNFGK
CTRSYHATCA LLAGVQVEQG QVAVIADDGN QYSIPSVDLK CKYHRQKKPS WMASGESPDY
DRKLIQTARG LVAGDLVQFQ ADKEINGAIV LQNRPEERTL LVKVLPRGSN FSPLAPGTRP
LPAHLARKPE ARKELESAVP VAGNPFGDGR SPYQWAEFET VDSTNHPNHQ SAPPSTQVDL
SKSEQIWYYL GESSTECRAQ YTHSPSVPVH NPRANFLDSV KSLGAVMARL PSYPHHLAPP
HHYGAGAGVG VGAGAPHPHL LSPLTASTHA PLAPPRPAPP TASSPAAMPS AYRSLPTQSA
RHAPYPQVTK SHHQQSLSRS QQIHNHHHHQ QQRQQTTNNL PANNFANVRE LIARRRLAQI
TDHANVFAGY NIVSPELVVE TLLGPMGSVP PPTGLEKLEL AMAQQRVQPR APDGTLLPLQ
PLNMRSEEVT QLLQMLRFSL VSHRDRLDVL QKKEAENIKQ EATNGGSLAA TKLPRKYAYL
EQQREQVPTV YQSPYDMPSG FTEYAQKTFG LTPCQPELPK PSLANDYFAS LSPEDQEKIL
KTCGSFVQRA IERSASHSRQ SSASNLRLAS ALAQQTENPT IDITTVEDMP FPNLDFPLHA
DSPCSSFSRS HLRFQSPNDF TNHGPETHHD HHDLFGDQQA NTRFWQHGPW AAGDGNTPNE
ETRPFFGPHE RLKHDYASSD ISLGRGGPGS LHSVDMAGFG LDGTDDLCNV LSP
//
