ID A0A9W9H0T9_9EURO Unreviewed; 1402 AA.
AC A0A9W9H0T9;
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=N7515_004810 {ECO:0000313|EMBL:KAJ5135532.1};
OS Penicillium bovifimosum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=126998 {ECO:0000313|EMBL:KAJ5135532.1, ECO:0000313|Proteomes:UP001149079};
RN [1] {ECO:0000313|EMBL:KAJ5135532.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 22155 {ECO:0000313|EMBL:KAJ5135532.1};
RA Petersen C.;
RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAJ5135532.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 22155 {ECO:0000313|EMBL:KAJ5135532.1};
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:KAJ5135532.1}.
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DR EMBL; JAPQKL010000004; KAJ5135532.1; -; Genomic_DNA.
DR RefSeq; XP_056522504.1; XM_056665554.1.
DR GeneID; 81404724; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP001149079; 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:UP001149079};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 91..132
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 354..517
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 597..722
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1402 AA; 156356 MW; 6BD759FF32803CFE CRC64;
MMAATLDQSQ RDSLAAGSIL DSASITPPHS ATGKKEVPEG VPSDLSDLEL DQRTAPELDT
AKIDTDMEGT EQKAEEVEEI EPDHYYGGGK VPVFKPTMDQ FRDFQGFINK IDKYGMQAGI
VKVIPPKEWS ESLPPLDEAV KKIRVKNPIM QEFHGSYGTY TQANIERQRS YNLPQWKGLC
EESSHQPPAR RGERRRNQER VNRAAPTPRP PSARPEGQKR RPGRPPKRSN QSKIKEEPPA
DDAEKSRLEG PPTPVSPETN PVQPKTEDLS EGESLPTTKP KGRQPKSVTS RRKNNRGETA
EQVDEEAYKG FDYRIQDHEE YTAERCEELE TNYWKSLMYN NPMYGADMPG SLFEDSTETW
NVAKLPNLLD VLGQKVPGVN TAYLYLGMWK ATFAWHLEDV DLYSINYIHF GAPKQWYSIS
QEDAPRFEQA MRSIWSSDAK NCDQFLRHKT YLVSPSLLKS QYGITVNRLI HYEGEFVITF
PYGYHSGYNL GYNCAESVNF ATEQWLDYAR IAKKCHCEAD SVWIDVDEIE RKLRGESTPE
YYGEFENEFD GFEGPTDLLT PPRSVPEKTS TRGRKRKNPD DGPSTKRPKI HPAGPRKLPC
LLCPNDLDYE DLLPTEDGKG HAHRRCAAFI EETTILHDAS GREVVCDIDK IPKARLGLKC
LFCREVRGAC FQCNFGKCTR AYHATCALLA GVQVEHGAIA VIADDGCQYS IPSVDLKCKF
HRQKRPSGVL SESSDLDRRV IESARRLVQG NLIQFQADKE INGAIVLENR HSERSLLLKV
LPRGDVIEMP YRWMLVVRKS NFIPLGLGIQ PLPAHLARKP EQRKELESAV PAAGSAFGDA
GSPYQWAEFE TVDATRNEFA PLSTVNLQPG EQMWYYLGAQ STESRAQYTH NPSVSIHNPR
ANFLDSVKSL GVGVTARASK ISPHHQFHYA ATAPAPPYQR NLQNQQNLYQ QKHQSNVNSP
HLQSRPPSSA LQHLAPPPPP IPAARAAAAG APAMPSAFRT LPNQSARHAP YPSVAKSHAQ
QQHHLPSTST FANVRELIAR RRLAQITDHA NVFAGYNIVS PELVVETLLG PMGSIPPANG
LEKLELAMAQ QRVQPRAADG TLLPPQTLNM RSEEVTRLLQ MLRFSLVSHR ERLDVIQKKE
SEGIKLETID RGSVAAAKMP GKYAYLDQQR SLAPNVYQSP YNMPSGLSEY AKSTYGLVPA
ADDPPKVSLA NDYFDSLSPE LQQKIVKACG SSVQRAIARS TSHSRQSSSS NLRLSAALAQ
QTENPTIDIT TVEDPPMLSG LDMPLHADSP CSSFGRSHLR FQSPNEFPIH GPDPHPDHHD
LFGDQQANTR FWQNGPWVTG DGNTPNEEHR PFFGPHIFGP HERLKHDYAS SDVSMGKGPG
SLHSVDMAGF GPDLNDDLGL SP
//
