ID A0A9W4KNS8_9EURO Unreviewed; 1406 AA.
AC A0A9W4KNS8;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 8.
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=PEGY_LOCUS9080 {ECO:0000313|EMBL:CAG8908225.1};
OS Penicillium egyptiacum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1303716 {ECO:0000313|EMBL:CAG8908225.1, ECO:0000313|Proteomes:UP001154252};
RN [1] {ECO:0000313|EMBL:CAG8908225.1}
RP NUCLEOTIDE SEQUENCE.
RA Branca A.L. A.;
RL Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases.
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:CAG8908225.1}.
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DR EMBL; CAJVRC010000892; CAG8908225.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP001154252; 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:UP001154252};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 89..130
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 352..515
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 595..720
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1029
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 23..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..292
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1406 AA; 156639 MW; 8651CD772EB19C6E CRC64;
MMATALDQSQ RGSLGGDPVV ESVSITPPQS ANGKKEAPEG VPSELSDLEL DHQSAPAPDT
INIKQEEVEE KAEDVEEIEP DHYYGGGKVP VFKPTMDQFR DFQGFINKIN KYGMQAGIVK
VVPPKEWSES LPTLDEAVKK IRVKNPIMQE FHGSHGTYTQ ANIERQRSYN LPQWKGLCEE
SSHQPPARRG ERRRNQERAN RAAPTPRPPS ARPEGQKRRP GRPPKRANQV KVKEEPPADD
TEKSRLEGPP TPVSPETNPV QPKTEDLSEG ESLPTTKPKG RQPKSVTSRR KNNRGDAMDQ
VDEEAYTGFD YRIHDHEEYT AERCEELETN YWKSLMYNNP MYGADMPGSL FEDSTETWNV
AKLPNLLDVL GQKVPGVNTA YLYMGMWKAT FAWHLEDVDL YSINYIHFGA PKQWYSISQE
DAPRFEQAMR SIWSSDAKNC DQFLRHKTYL VSPSLLKSQY GITVNRLVHY EGEFVITFPY
GYHSGYNIGY NCAESVNFAT EQWLDYARIA KKCNCEADSV WIDVDEIERK LRGESTPEYY
GEFESEFDGF EGASDLLTPP RSVPEKTSTR GRKRKNPDDG PNSKRPKLHP EGPRKLPCLL
CPNNLDYEDL LPTEDGKGHA HRRCAAFIEE TTILRDASGT EVVCDIDKIP KARLGLKCLF
CREVRGACFQ CNFGKCTRAY HATCALLAGV QVEHGAIAVI ADDGTQYSIP SVDLKCKFHR
QKRPNGVLGE SSDVDRRVIE SARRLVQGNL IQFQADKEIN GAIVLENRPS ERSLLLKVLP
RGXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXAH LARKPEQRKE LESAVPAAGS
AFGDARSPYQ WAEFETVDGT RNQFAPLSTV NLQGEQMWYY LGMQSTESRA QYTHNPSVSI
HNPRANFLDS VKSLGMGVSA RASKISPHHF HYAATAPAPP YQRNLNKPNQ HQNQQNIYSQ
ANVHTPQLQS RPPSSALHLA PLPPSVPVAG AAAGAPAMPS AFRTLPNQSA RHAPYPSVVK
SHAQQQHHLP STNTFANVRE LIARRRLAQI TDHANVFAGY TIVSPELVVE TLLGPMGSIP
PANGLEKLEL AMAQQRVQPR AADGTLLPPQ TLNMRSEEVT RLLQMLRFSL VSHRERLDVI
QKKESEGIKQ ETVDRGSVAA AKMPGKYAYL DQQRSLAPNV YQSPYNMPSG LSEYAKATYG
LVPAADDPPK PSLANDYFNN LSEEHQEKIL KACGSFVQRA IERSASHSRQ SSSSNLRLSA
ALAQQTENPT IDITPVEDPP LLSGLDMPLH ADSPCSSFGR SHLRFQSPNE FPIHGPDPHP
DHHDLFGDQQ ANTRFWQNGP WVGGDGNTPN DENRPFFGPH LFGPHDRLKH DYASSDISLG
KGPGSLHSVD MAGFGPDMND DLGLSP
//
