ID A0A317VWZ4_9EURO Unreviewed; 1475 AA.
AC A0A317VWZ4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 02-APR-2025, entry version 21.
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=BO70DRAFT_397705 {ECO:0000313|EMBL:PWY77418.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY77418.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY77418.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY77418.1,
RC ECO:0000313|Proteomes:UP000247233};
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 (DEC-2016) 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:PWY77418.1}.
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DR EMBL; MSFL01000018; PWY77418.1; -; Genomic_DNA.
DR RefSeq; XP_025397991.1; XM_025546728.1.
DR STRING; 1448321.A0A317VWZ4; -.
DR GeneID; 37068965; -.
DR VEuPathDB; FungiDB:BO70DRAFT_397705; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000247233; 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:UP000247233};
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 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..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..31
FT /note="Polar residues"
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 941..951
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..969
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1030
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1087
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1101
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1475 AA; 163817 MW; FF801921828EF583 CRC64;
MAAALDQPLF ESIAGGPATD ATSITPPQSV NGKKDIPDGV SSELSDLELD PNAPGAQDIP
SVEADEDEIE PDHYYGGGKI PVFKPTMDQF RDFQSFINKV DEYGMRSGIV KVIPPKEWTD
ALPPLDDAVR NIRVKNPIMQ EFHGSHGTYT QANIERQRSY NLPQWKALCE ESSHQPPARR
GERRKNQERT SRAPPVPRAQ SVRSDSQKRR AGPGRPPKRT NQLKIKEEPQ ADEGLDKVKP
EGPPTPVSPE SNPVEAKTED LSDGESLPGP KPKGRQPKSS VTSRRKHNKG DAIDYVDEEA
FRDFDYRIHD NDEYTAERCE ELETAYWKSL MFNNPLYGAD MPGSLFDDDI TTSWNVARLP
NLLDVIGQKV PGVNTAYLYL GMWKATFSWH LEDMDLYSIN YIHFGAPKQW YSISQEDAPR
FEQAMKSIWT SDAKSCDQFL RHKTYLVSPN LLKSQYGITV NKLVHYEGEF VITYPYGYHS
GYNLGYNCAE SVNFATEKWL DYGRVAKKCN CESDSVWIDV DEIERKLRGE ATPEYFGEYE
SDLDEVEGAS DLLTPPRSVP EKSSTRGRKR KTVGETTKAK RMRVNMEVPR KIPCVLCPNN
LDYEDLLPTE DGKSHAHRRC ALYTEETTIL RDETGKEVVC DVDKIPKARM GLKCLFCREV
RGACFQCNFG KCTRSYHATC ALLAGVQVEQ GLVGVIADDG NQYSIPSVDL KCKYHRQKKP
SWLASTETPD FDRKLIQTAR GLVAGDLVQF QADKEINGAI VLQNRPEERA LLVKVLPRGD
VIELPYRWTL VVRRSNFSPL APGTRPLPAH LARKPEARKE LESAVPVAGN PFGDGRSPYQ
WAEFETVDST NQPKQAGAPP PTQVDLSKGE QLWYYLGESS TECRAQYTHN PSVAVHNPRA
NFLDSVKSLG AVMARLPPSI SYAPHHHLAP PPHHYAAAPH RPAPQAPPTL PPHHLAGGGA
PPPPPPLPPT ASIVSAATTA AVAASAATSA TTAAAAAASR RPSLLQHPPL APPRPAPSSA
AAPPAAMPSA YRSLPTQSAR HAPYPQVTKA PHHHHLPSGS RPQPLHHHHH LHQQSQQPPP
PTPPQPQPQQ QQQQQQQQQT NNPPPNNFAN VREIIARRRL VQITDHANVF AGYTIVSPEL
VVETLLGPMG SVPPPNGLEK LELAMAQQRV QPRAPDGTLL PLQPLNMRSE EVTRLLQMLR
FSLVSHRDRL DVLQKKEPEH IKQEPVNGGL PASKLPRKYA YLEQQREQVP TVYRSPYDMP
SGFTEYAQKS YGLTPCEPEL PKPSLANDFF ASLSPEDQEK ILKTCGSFVQ RAIERSASHS
RQSSASNLRL ASALAQQTEN PTIDITTVED MHFPNLDFPL HADSPCSNFS RSHLRFQSPN
EFAPHGPEPH HDHHDLFGDQ QANTRFWQHG PWAAGDGNTP NEETRPFFGP HERLKHDYAS
SDISLGRGGP GSLHSVDMAG FGMDNAEDPL GVLSP
//
