ID A0A1L9SRV4_9EURO Unreviewed; 1435 AA.
AC A0A1L9SRV4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 02-APR-2025, entry version 23.
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=ASPZODRAFT_1046496 {ECO:0000313|EMBL:OJJ49854.1};
OS Penicilliopsis zonata CBS 506.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicilliopsis.
OX NCBI_TaxID=1073090 {ECO:0000313|EMBL:OJJ49854.1, ECO:0000313|Proteomes:UP000184188};
RN [1] {ECO:0000313|Proteomes:UP000184188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 506.65 {ECO:0000313|Proteomes:UP000184188};
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; KV878337; OJJ49854.1; -; Genomic_DNA.
DR RefSeq; XP_022584364.1; XM_022720867.1.
DR STRING; 1073090.A0A1L9SRV4; -.
DR GeneID; 34607332; -.
DR VEuPathDB; FungiDB:ASPZODRAFT_1046496; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000184188; 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 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:UP000184188};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..35
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 270..433
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 534..659
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 84..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..117
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..505
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..923
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..934
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..978
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..989
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1224
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1312
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1435 AA; 159398 MW; FB9F3741C7853927 CRC64;
MDQFRDFQAF IQKVDKYGMQ SGIVKVIPPK EWTGSLPALD EAVKKIRVKN PIMQEFHGSH
GTYTQANIER QRSYNLPQWK ALCEESSHQP PARRGERRRN QERAPRATPT PRPATTRSSE
PQQKRGPGRP PKRSNQQQQQ QQQQVKIKEE PPADDGLVDK TKPEGPPTPV SPESNPVEAK
SEELSEGESL PAPKPKGRQP RSVTARRKTN NRGDAIDAID EEAFKGFDYH ITDGEDYTAE
RCEELETAYW KSLMFNNPLY GADMPGSLFD DSTTSWNVAR LPNLLDVLGQ KVPGVNTAYL
YLGMWKATFA WHLEDVDLYS INYIHFGAPK QWYSISQADA PRFEQAMRSI WPSDAKNCDQ
FLRHKTYLVS PSILKSQYGI TVNRLVHYEG EFVITYPYGY HSGFNLGYNC AESVNFATEQ
WLDYGRIAKK CHCEADSVWI DVEEIQRKLR GESTPEYYYY GELESELDEM DGASDLLTPP
RSVPEKAGSS SSTITTTTTT TTTGGSTRGR KRKLDNGEPR TGKRTRMGPD ASRKLPCVLC
PNNLDYEDLL PTEDGKAHAH RRCALYIEET TILRDGTGRE VVCDIDQIPK ARLGLKCLFC
REVRGACFQC NFGKCTRAYH ATCALLAGVQ VEMGSLAVVA DDGQTYSVPS VDLKCKFHRQ
KRQAWYPGET ADTDKRLIER ASRLIQGDLV QFQADKEING AIVLQNRPEE RTALLKVLPR
GDIIELPYRW MLIVRRSNFP PLPSGIAPLP AHLARKPDPR RDLDTGLPLP GRPFCDADAP
YQWAEFESVA LRASSDAAPP VLVDLDRHEQ LWHYLGASST ECRAQYTHNP SLPVHNPRAN
FLDSVKSLGA LAAAGRLPPS SSSSSSLSSS HPHHHLYAAV TAAAAAPPSS LPLQQRPPPS
AAAAAMPPAY HRSLPNNRNN NSLHHSHHHH HRHAPYPSVS VAKTLPPHHH LTTTTTTTTN
NNNNNNNNNH NNNNTTTGGN NGVNNGIGGG SDLPTHTFAN VRELIARRRL AQITEHANVF
AGYPIISPEQ VVEILLGPMG SVPPPTGLEK LELAMAQRRV QPRAADGTLL PLQPLNMRSE
EVTRLLQMLR FSLVSHRERL DVLHKRDAAR PETTVDKAAI TAAKLPGKYA YLDQQRTQVP
TVYQSPYDMP SGFSAYAQQT YGLVPAPPAP DRPVLPSLAN DFFARLTPDQ QELILRTCGS
FVQQRATSSR HHSRQGSSSS NLRLSAALAR QTDHPIIDIT PAAAATGGGP TIILDADGSD
VHPSLRPNDD GSDGHHLNHH HHHHPQHPQH PQHHPHLHHP HLSTHHLSSH HHLSLAALDP
PLHADSPTSS FSRSHLRFPS PNHDFVPHAD SQDHHDLFGD QQANTRFWQH GPWAAGDGNT
PNEENRPFFG PHERLKHDYA SSDISLGRGP GSLHSVDMAG FGLDVPDDLC ADLSP
//
