ID A0A1L9TWB6_9EURO Unreviewed; 1413 AA.
AC A0A1L9TWB6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 02-APR-2025, entry version 25.
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=ASPSYDRAFT_140238 {ECO:0000313|EMBL:OJJ63658.1};
OS Aspergillus sydowii CBS 593.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ63658.1, ECO:0000313|Proteomes:UP000184356};
RN [1] {ECO:0000313|Proteomes:UP000184356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878582; OJJ63658.1; -; Genomic_DNA.
DR RefSeq; XP_040707464.1; XM_040841028.1.
DR STRING; 1036612.A0A1L9TWB6; -.
DR GeneID; 63757101; -.
DR VEuPathDB; FungiDB:ASPSYDRAFT_140238; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000184356; 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:UP000184356};
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 351..514
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 592..717
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..974
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1027
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1413 AA; 157343 MW; D4D887CC9AC19592 CRC64;
MAATIDRPPL EQIAGGPATD AASITPPHSV KGKKEAPDGA PSELSDLELD SKTTGAQESP
SVEDEDEEIE PDHYYGGGKI PVFRPTMNQF RDFQAFIDKV DKYGMRSGIV KVIPPKEWSD
ALPALDEAVK KIRVKNPIMQ EFHGSHGTYT QANIEKQRSY NLPQWKALCE DGSHQPPARR
GERRRNQERA NRAPSAPKPQ ATRSDTPKRG PGRPPKRSNQ AKTKEEAVKI KEEPTADDSI
DNIKQEGPPT PVSPESNPVE AKSEALSDGE SLPAPKSRAR QPKSVTARRK QNKGDIIDHI
DEEAYKDFDY RIHDNQAYTY ERCEELETAY WKSLMFNNPM YGADMPGSLF DENTTSWNVA
KLPNLLDVIG QKVPGVNTAY LYLGMWKATF AWHLEDVDLY SINYIHFGAP KQWYSISQED
APKFEQAMKS IWPSDAKTCG QFLRHKTYLV SPSLLKSQYG ITVNKMVHYE GEFVITYPYG
YHSGYNLGYN CAESVNFATE KWLDYGRVAK KCNCESDSVW IDVDDIERKL RGESTPEYYG
EFDSELDAVE GASDLLTPPR SVPEKNSTRG RKRKLDGDMA KVKRVKVDYP KKMPCLLCPN
DLDYEDLLPT EDGKSHIHRR CALYTEETSI LRDESGKEVV CDIEHIPKAR MGLKCLFCRE
VRGACFQCNF GKCTRSYHAT CALLAGVQVE EGAVTVVADD GNQYSVPSVD LKCKYHRQKK
PSWMTSSESP DNDRKLIETA RHLVIGNLLQ FQVDKEISGA VVLENRPTER TLLVKVLPRG
DVIELPYRWM LVVRRSNFAP LATGIKPLPA HFARKPEARR ELESALPVAG NPFGDGRSPY
QWAEFETVES TNRASAPPMV QVNLDKMEQI WYYLGQSSTE CRAQYTHNPS VAIHNPRSNF
LDSVKSLGAV MARLPSYPHQ RLPPYVLTAP HPHLLSSAAA TTTASAVAVT AAAAAAASRP
SLPQRPPFAP PPRSSPAAPT SAAVAASAMP SAYRSLPNQS ARHAPYPQLT KAHIQSQQQH
SHQQQQQNTN GSVTTNNSHL PVNNFAGVRE IIARRRLAQI TDHANVFAGY TIVSTELVVE
TLLGPMGSVP PSNGLEKLEL AMAQQRVQPR ASDGTLLPMQ PLNMRSEEVT RLLQMLRFSL
ISHRDRLDVL QKKESENLKQ ETANKTNGAA AKVPQKYAYL EQQREQAPTV YQSPYDMPSG
FTEYARTTFG LTRAEPELPI PSLANDYFAS LSPENQEKIL KTCGSFVQRA MERSAPHSRQ
SSASNLRLAS ALAQQTENPT IDITTVEDMP LSGLDFPLRA DSPCSNFSRS HLRFHSPNDF
TNHGTEVHHD HHDLFGDQQA NTRFWQHGPW AAGDGNTPNE ESRPFFGPHE RLKHDYASSD
ISLGRGGPGS LHSVDMAGFG LDNPDDLCGA LSP
//
