ID A0A124BXA1_ASPNG Unreviewed; 1435 AA.
AC A0A124BXA1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=ABL_04412 {ECO:0000313|EMBL:GAQ41751.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ41751.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ41751.1}.
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DR EMBL; BCMY01000006; GAQ41751.1; -; Genomic_DNA.
DR PaxDb; 5061-CADANGAP00006692; -.
DR VEuPathDB; FungiDB:An08g04965; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1227632; -.
DR VEuPathDB; FungiDB:ATCC64974_102410; -.
DR VEuPathDB; FungiDB:M747DRAFT_66496; -.
DR OMA; NQERVNR; -.
DR Proteomes; UP000068243; 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; IPR001965; Znf_PHD.
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 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 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 348..511
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 591..716
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1006
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1435 AA; 159564 MW; 29F0E61BA5313D8A CRC64;
MMAAALDQPP FDPIAGAPAT DAASITPPQS VNGKKEVPDG VPSELSDLEL DPNVNGAQEI
PSVEADDEEI EPDHYYGGGK IPVFKPTMDQ FRDFQSFINK VEEYGMRSGI IKVIPPKEWT
DSLPPLDEAV KKIRVKNPIM QEFHGSHGTY TQANIERQRS YNLPQWKALC EESSHQPPAR
RGERRRNQDR VTRAPSAPKT QNARSDSQKR RAGPGRPPKR ANQVKVKEEP PADEGLDKIK
PEGPPTPVSP ESNPVEAKNE ELSDGESLPG PKPKGRQPKS VTSRRKHNKG DAIDYVDEEA
FQDFDYRIDD SQDYTYERCE ELETNYWKSL MFNNPMYGAD MPGSLFDDNI TTSWNVARLP
NLLDVLGQKV PGVNTAYLYL GMWKATFAWH LEDVDLYSIN YIHFGAPKQW YSISQEDAPR
FEQAMKSIWQ SDAKNCDQFL RHKTYLVSPN LLKSQYGITV NKLVHYEGEF VITYPYGYHS
GYNLGYNCAE SVNFATEKWL DYGRVAKKCN CEADSVWIDV DEIERKLRGE ATPEYFGEYE
SDLDEIEGAS DLLTPPRSVP EKTSTRGRKR KNDGETTKAK RMRVAMDVPR KIPCVLCPNN
LDYEDLLPTE DGKSHAHRRC ALYTEETSIL RDESGKEVVC DVDKIPKARM GLKCLFCREV
RGACFQCNFG KCTRSYHATC ALLAGVQVEQ GQIAVIADDG NQYSIPSVDL KCKYHRQKKP
SWMASGESPD YDRKLIQTAR GLVAGDLVQF QADKEINGAI VLQNRPEERT LLVKVLPRGD
VIELPYRWML VVRRSNFSPL APGTRPLPAH LARKPEARKE LESAVPVAGN PFGDGRSPYQ
WAEFETVDST NHPNHQSAPP STQVDLSKSE QIWYYLGESS TECRAQYTHS PSVPIHNPRA
NFLDSVKSLG AVMARLPSSY PHHLAPPHHY AGAGVGAPHP HLLSPLTASA AAAAVSAAAA
TTAAATTTTT TTSAAAAAAA AASRRPSLLQ HAPLAPPRPA PPTASSPAAM PSAYRSLPTQ
SARHAPYPQV TKSHHHQSLS RPQQLHNHLH HQQQQQQTPN NLPANNFANV RELIARRRLA
QITDHANVFA GYTIVSPELV VETLLGPMGS VPPPTGLEKL ELAMAQQRVQ PRAPDGTLLP
LQPLNMRSEE VTRLLQMLRF SLVSHRDRLD VLQKKESENI KQEAANGGSL AATKLPRKYA
YLEQQREQVP TVYQSPYDMP SGFTEYAQKT FGLTPCQPEL PKPSLANDYF ASLSPEDQEK
ILKTCGSFVQ RAIERSASHS RQSSASNFRL ASALAQQTEN PTIDITTVED MPFPNLDFPL
HADSPCSSFS RSHLRFQSPN DFTNHGTETH HDHHDLFGDQ QANTRFWQHG PWAAGDGNTP
NEETRPFFGP HERLKHDYAS SDISLGRGGP GSLHSVDMAG FGLDGTDDIC NVLSP
//
