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Database: UniProt
Entry: A0A9W9XJ66_9EURO
LinkDB: A0A9W9XJ66_9EURO
Original site: A0A9W9XJ66_9EURO 
ID   A0A9W9XJ66_9EURO        Unreviewed;      1379 AA.
AC   A0A9W9XJ66;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   28-JAN-2026, entry version 11.
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=N7463_009885 {ECO:0000313|EMBL:KAJ5493798.1};
OS   Penicillium fimorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1882269 {ECO:0000313|EMBL:KAJ5493798.1, ECO:0000313|Proteomes:UP001149954};
RN   [1] {ECO:0000313|EMBL:KAJ5493798.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 29495 {ECO:0000313|EMBL:KAJ5493798.1};
RA   Petersen C.;
RL   Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAJ5493798.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 29495 {ECO:0000313|EMBL:KAJ5493798.1};
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:KAJ5493798.1}.
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DR   EMBL; JAPWDS010000006; KAJ5493798.1; -; Genomic_DNA.
DR   OrthoDB; 9547406at2759; -.
DR   Proteomes; UP001149954; 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:UP001149954};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          88..129
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          349..512
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          592..717
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..11
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..227
FT                   /note="Basic 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"
SQ   SEQUENCE   1379 AA;  154057 MW;  9524616817CAB805 CRC64;
     MATVLDQSQC ESLGGNPVVQ SVSITPPQSA NGKKEAPEGV PSELSDLELD HQSAPAPDTT
     KIKQEEMEEK VEEIEEIEPD HYYGGGKVPV FKPTMDQFRD FQSFINKINK YGMQAGIVKV
     IPPKEWSESL PPLDEAVKKI RVKNPIMQEF HGSHGTYTQA NIERQRSYNL PQWKGLCEES
     SHQPPARRGE RRRNQERVNR AAPTPRPPSA RPEGQKRRPG RPPKRTNKVK EEPPADDAEK
     SRLEGPPTPV SPETNPVQPK TEDLSDGESL PTTKPKGRQP KSVTSRRKNN RGDAMDQFDE
     EAYTGFDYRI HDHEEYTAER CEELETNYWK SLMYNNPMYG ADMPGSLFED STETWNVAKL
     PNLLDVLGQK VPGVNTAYLY MGMWKATFAW HLEDVDLYSI NYIHFGAPKQ WYSISQEDAP
     RFEQVMRSIW SSDAKNCDQF LRHKTYLVSP SLLKSQYGIT VNRLVHYEGE FVITFPYGYH
     SGYNVGYNCA ESVNFATEQW LDYARIAKKC HCEADSVWID VDEIERKLRG ESTPEYYGEF
     ESEFDGFEGA SDLLTPPRSV PGKTSTRGRK RKNPGDGPNS KRPKLHPEGP RKLPCLLCPN
     NLDYEDLLPT EDGKGHAHRR CAAFIEETTI LRDASGTEVV CDIDKIPKAR LGLKCLFCRE
     VRGACFQCNF GKCTRAYHAT CALLAGVQIE HGAIAVIADD GTQYSIPSVD LKCKFHRQKR
     PNGVLGESSD VDRRVIESAR RLVQGNLIQF QADKEINGAI VLENRPSERS LLLKVLPRGD
     VIEMPYRWML VVRKSNFTPL ALGIQPLPAH LARKPERKEL ESAVPAAGSA FGDSRSPYQW
     AEFETVDGTR NQFAPLRTVN LEGEQIWYYL GMQSTESRAQ YTHNPSVSIH NPRANFLDSV
     KSLGMDVSAR ASKISPHHFH YAATASAPPY RNLNQQNIYS NVNALQSRPP SSALQNAPPP
     PFIPATGAAA GTAMPSAFRT LPQSARYAPY PSAKHAQQQH HLQSTNTFAN VRELIARRRL
     AQITDHANVF AGYTIVSPEL VVETLLGPMG SIPPANGLEK LELAMAQQRV QPRAADGTLL
     PPQTLNMRSE EVTRLLQMLR FSLVSHRERL DVIQKKESEG IKQETVDRGS VAAAKMPGKY
     AYLDQQRSLA PNVYQSPYNM PSGLSEYAKT AYGLVPAADD PPKPSLSNDY FNNLPQEHQE
     KILKACGSFV QRAIERSASH SRQSSSSNLR LSAALAQQTD NPTIDITPVE DPPLLSGLDM
     PLHADSPCSS FGRSHLRYQS PNEFPIHGPD PHPDHHDLFG DQQANTRFWQ NGPWVGGDGN
     TPNDETRPFF GPHIFGPHER LKHDYASSDI SLGKGPGSLH SVDMAGFGPD LNDDLGLSP
//
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