ID A0A9W9GQ99_9EURO Unreviewed; 1404 AA.
AC A0A9W9GQ99;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
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=N7476_001147 {ECO:0000313|EMBL:KAJ5331364.1};
OS Penicillium atrosanguineum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1132637 {ECO:0000313|EMBL:KAJ5331364.1, ECO:0000313|Proteomes:UP001147746};
RN [1] {ECO:0000313|EMBL:KAJ5331364.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 21472 {ECO:0000313|EMBL:KAJ5331364.1};
RA Petersen C.;
RL Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAJ5331364.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 21472 {ECO:0000313|EMBL:KAJ5331364.1};
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:KAJ5331364.1}.
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DR EMBL; JAPZBO010000001; KAJ5331364.1; -; Genomic_DNA.
DR Proteomes; UP001147746; 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:UP001147746};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..999
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1404 AA; 156339 MW; 5247CA74F2799A19 CRC64;
MSVAFDQPPL DALVSGPVVD SASITPPRSA NGKKDIPEGV PSELSDLELD QKSTQAPDEM
PIKQEEQEEQ EEQEIDIGPI EPDHYYGDGK IPVFKPTMDQ FRDFKKFINK IDGYGMKAGI
VKVVPPKEWT DSLTPLDEAV KSIRVKNPIM QEFHGSHGTY TQANIEKQRT YNLPQWKGLC
EESSHQPPAR RGERRRNQER GNRTANTPRP QSARPTGDGA KRRPGRPPKR GNQIKVKEEP
VDDADSSKPE GPPTPVSPES HPVETKSEDL SEGESLPPTK PKGRQPKSVT SRRKNNRGET
VDHFDEEAFK GFDYRIHDHE DYTAERCEEL ETAYWKSLMY NNPMYGADMP GSLFEDSVDS
WNVAKLPNLL DVIGQKVPGV NTAYLYLGMW KATFAWHLED VDLYSINYIH FGAPKQWYSI
SQEDAPKFEA AMRSIWSSDA KNCDQFLRHK TYLVSPSLLK SQYGITVNRL VHYEGEFVIT
FPYGYHSGYN IGYNCAESVN FATEKWLEYG RVAKKCHCEA DSVWIDVDEI ERKLRGESTP
EYYGEYDSDL EGFEGASDLL TPPRSVPEKT STRGQKRKNA GDGPRTKRIK LHLQGPRKIP
CLLCPNDLDY EDLLPTEDGK GNAHRRCASF IEETTILRDA SGNEVVCDID RIPKARLDLK
CLFCREVRGA CFQCNFGKCT RAYHATCALL AGVQVEHGSI AVIADDGQQY SLPSVDLKCK
FHRQKRPAGL LGESSDLDRR VIEAARRLVQ GVLIQFQVDK EINGAIVLQN RPEERSLLLK
VLPRGDVIEM PYRWMLVVRK SNFVPLAPGI PPLPAHLARK PERKELEAAI PVAGSAFGDT
GSPYQWAEFE TVDATRNSFA PLTVNLDKGE QVWHYLGAPS TESRAQYTHN PSVPIHNPRA
NFLDSVKSLG VAGVSARASK ISPHHHFRYA PTAPAPPYQQ NLYARQPQVK QQQQHHYLTP
SLQSRPPSFT SAPSLQHLAP PPHPAPAAGA AAGPAMPSAF RTLPNQSTRH APYPSVAKSH
QQQHHLPSTN TFANVRELIA RRRLAQITDH ANVFAGYTIV SPELVVETLL GPMGSIPPAN
GLEKLELAMA QQRVQPRAAD GTLLPPQTLN MRSEEVTRLL QMLRFSLVSH RERLDVIQKK
ESEGVKQETI DRGSVAAAKM PGKYAFLDQQ RALAPKVYQS PYNMPSGLSE YAKTTYGLIH
SEGEPPKSSL ANDFFNSLSQ VDKEKIMKTC GSFVQRAIDR STSHSRHSST GSNLRLSSAL
AQQTSNPTID ITTVDDPPLS GLDLPLHADS PGSSFGRSHL RFQSPNEFPI HGPDPHPDHH
DLFGDQQANT RFWQNGPWIA GDGNTPNDEN RTFFGPQFGP HERLKHDYAS SDISLGKGPG
SLHSVDMAGF GLDATDDLCG ELSP
//
