ID A0A9W9JV52_9EURO Unreviewed; 1398 AA.
AC A0A9W9JV52;
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=N7532_011633 {ECO:0000313|EMBL:KAJ5082590.1};
OS Penicillium argentinense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1131581 {ECO:0000313|EMBL:KAJ5082590.1, ECO:0000313|Proteomes:UP001149074};
RN [1] {ECO:0000313|EMBL:KAJ5082590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 30761 {ECO:0000313|EMBL:KAJ5082590.1};
RA Petersen C.;
RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAJ5082590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 30761 {ECO:0000313|EMBL:KAJ5082590.1};
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:KAJ5082590.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAPQKI010000011; KAJ5082590.1; -; Genomic_DNA.
DR RefSeq; XP_056469112.1; XM_056624124.1.
DR GeneID; 81363103; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP001149074; 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:UP001149074};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 86..127
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 349..512
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 593..718
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..974
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..996
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1398 AA; 155255 MW; FFE154010D1A5A42 CRC64;
MAATLDRTHP DPLAGGPVVD SASITPPHSA NGKKDVPEGV PSELSDLELD SKPAATHEEP
AIKQEEPEEQ VEEDIEPDHY YGGGKIPVFK PTMDQFRDFQ KFINKIDKYG MQAGIVKVVP
PKEWSESLSP LDEAVKSIRV KNPIMQEFHG SHGTYTQANI ERQRSYNLPQ WKALCEESNH
QPPARRGERR RNQERANRAA PTPRAQSSRP ESQKRRPGRP AKRGNQAKVK EEHAPDDADK
TKPEGPPTPV SPESIPVEPK SEELSEGESL PATKPKGRQP KSVTSRRKNN RGETVDHVDE
EAFKAFDYRI HDNEDYTADR CDELETAYWK SLMFSNPLYG ADMPGSLFDD SIESWNVAKL
PNLLDVLGQK VPGVNTAYLY LGMWKATFAW HLEDVDLYSI NYIHFGAPKQ WYSISQDDAP
KFEAAMRSIW SSDAKNCDQF LRHKTYLVSP SLLKSQYGIT VNRLVHYEGE FVITFPYGYH
SGYNIGYNCA ESVNFATERW LDYGRIAKKC HCEADSVWID VDEIERKLRG EATPEYYGDF
ESELDGFEGA SDLLTPPRSV PEKASSTRGR KRKITGDGPR TKRSKIHQEG PRVFPCLLCP
NDLDYEDLLP TEDGKGHAHR RCASFIEETT ILRDAAGNEV VCDIGLIPKA RLGLKCLFCR
EVHGACFQCN FGKCTRAYHA TCALLAGVQV EHGSIAVIAD DGEQYALPNV DLKCKFHRQK
RPAGLLGESS DLDRRVIEAA RRLNSGELIQ FQADKEINGA IVLQNRPEER TLLVKVLPRG
DVIEMPYRWM LVIRKSNYAP LAPGIQPLPA HLVRKPEQRK DYEAAVPVAG SAFCDEKAPY
HWAEFETVDA ARNQLAPPVT VSIDRPEQIW YYLGAQSTEN RAQYTHNPSV PVHNPRANFL
DVVKSLGVAG AARASKISPH HLFHYAPTAP APPFQQNLYA QHRPQLQHKH SFLNADTPHL
SSRPPSSSAS LQHLAPPPPP APAAGAAAAG PAMPSAFRTL PNQSARHAPY PSIAKSQIQQ
QHHLPSTNTF ANVRELIARR RLAQITDHAN VFAGYTIVSP ELVVETLLGP MGSIPPATGL
EKLELAMAQQ RVQPRAADGT LLPPQTLNMR SEEVTRLLQM LRFSLVSHRE RLDVIQKKES
EGVKQETVDR GSIAAAKMPG KYAFLDQQRA LAPNVYQSPY NMPSGLSEYA KKTYELIPSA
DEPPKESLAN GFFASLSQAD KDKIMKTCGS YVQRAIDRSA SHSRHSSTAS NLRLSTALAQ
QTENPTIDIT TVEDPPISGL DLPLHADSPC SSFGRSHLRL QSPGDFPIHG PDPHPDHHDL
FGDQQANTRF WQNGPWAAGD GNTPNEENRP FFGPHERLKH DYASSDISLG KGPGSLHSVD
MAGFGFDTAE DLCAGLSP
//
