ID A0A9X0B821_9EURO Unreviewed; 1385 AA.
AC A0A9X0B821;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 9.
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=N7509_007087 {ECO:0000313|EMBL:KAJ5391597.1};
OS Penicillium cosmopolitanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1131564 {ECO:0000313|EMBL:KAJ5391597.1, ECO:0000313|Proteomes:UP001147747};
RN [1] {ECO:0000313|EMBL:KAJ5391597.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 29677 {ECO:0000313|EMBL:KAJ5391597.1};
RA Petersen C.;
RL Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAJ5391597.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 29677 {ECO:0000313|EMBL:KAJ5391597.1};
RX PubMed=36726175;
RA Petersen C., Sorensen T., Nielsen M.R., Sondergaard T.E., Sorensen J.L.,
RA Fitzpatrick D.A., Frisvad J.C., Nielsen K.L.;
RT "Comparative genomic study of the Penicillium genus elucidates a diverse
RT pangenome and 15 lateral gene transfer events.";
RL IMA Fungus 14:0-0(2023).
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:KAJ5391597.1}.
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DR EMBL; JAPZBU010000008; KAJ5391597.1; -; Genomic_DNA.
DR RefSeq; XP_056487275.1; XM_056631724.1.
DR GeneID; 81370704; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP001147747; 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:UP001147747};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 90..131
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 353..516
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 596..721
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..981
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1385 AA; 153837 MW; C471AC45E4207E54 CRC64;
MAATLDQPHL DPLGGGPVVD SASITPPHSA NGKKYAPEGV PSELSDLELD AKSAAALDEP
AIKQEEQEEP VVEVEEEDIE PDHYYGGGKI PVFKPTMDQF RDFQKFINKI DKYGMQAGIV
KVVPPKEWTE SLSPLDDPIK SIRVKNPIMQ EFHGSHGTYT QANIERQRSY NLPQWKGLCD
ESSHQPPARR GERRRNQERA NRAASTPRAQ SSRPESQKRR PGRPAKRGNQ VKVKEEPPAD
DVEKSKPEGP PTPVSPESNP IELKSEELSE GESLPAAKPK GRQPKSVTSR RKNNRGDTVD
NVDEEAFKDF DYRIHDNEDY TAERCEELET AYWKSLMFNN PMYGADMPGS LFDDSVESWN
VAKLPNLLDV LGQKVPGVNT AYLYLGMWKA TFAWHLEDVD LYSINYIHFG APKQWYSISQ
EDAPKFEAAM RSIWSSDAKN CDQFLRHKTY LVSPSLLKSQ YGITVNRLVH YEGEFVITFP
YGYHSGYNIG YNCAESVNFA TERWLDYGRI AKKCHCEDDS VWIDVDEIER KMRGETTPEY
YVDFESEFDG FEGASDLLTP PRSVPEKTST RGRKRKITGD GPSTKRSKLH MEGPRKLPCL
LCPNNLDYED LLPTENGKGH VHRRCALFIE ETSILRDESG NEVVCDIDLI PKARLGLKCL
FCREVRGACF QCNFGKCTRA YHATCALLAG VQVEHGAIAV IADDGVHYTL PSVDLKCKFH
RQKRPAGLLG ESSDLDRRVI EAARRLTQGD LIQFQVDKEI NGAIVLQNRP QERALLLKVL
PRGDVIEMPY RWMLVVRKSN FAPLAPGIQP LPAHLVRKPE QRKDFEAAVP LAGSAFGDGR
SPYQWAEFET VDAARNQFAP PVTVTIDRPE HLWYYLGTQS TESRAQYTHN PTVPIHNPRA
NFLDSVKSLG VAGAGAGAAR ASKISPHHLF QHAPTAPAPP YQQILYAQHP ALLQHKHASL
NANTPHLPSR PPSSSASLTH LAPPPPPVLA AGAAAAGPAM PSAFRTLPNT SARHTPYPSV
IKSHVQQQHH LPSTNTFANV RELIARRRLA QITDHANVFA GYTIVSPELV VQTLLGPMGS
IPRPMVWRSS SSRWPSSGCS PGLPMMLRFS LVSHRERLDV IQKKESEGIK LETVDRGSIA
AAKMPGKYAF LDQQRAMAPN VYQSPYNMPS GLSEYAKTTY ELVPAPDEPP KESLANDFFA
SLSQIDKEKI MKTCGSFVQR AIERSASHSR HSSTASNLRL SSALAQQTEN PTIDITTVED
QPISGLDLPL HADSPCSSFG RSHLRLQSPG DFPIHGPDPH PDHHDLFGDQ QANTRFWQNG
PWTAGDGNTP NDENRPFFGP HERLKHDYAS SDISLGKGGP GSLHSVDMAG FGFDTAEDLC
AGLSP
//
