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Database: UniProt
Entry: A0A9W9K8Y6_9EURO
LinkDB: A0A9W9K8Y6_9EURO
Original site: A0A9W9K8Y6_9EURO 
ID   A0A9W9K8Y6_9EURO        Unreviewed;      1399 AA.
AC   A0A9W9K8Y6;
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=N7456_008041 {ECO:0000313|EMBL:KAJ5097320.1};
OS   Penicillium angulare.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=116970 {ECO:0000313|EMBL:KAJ5097320.1, ECO:0000313|Proteomes:UP001149165};
RN   [1] {ECO:0000313|EMBL:KAJ5097320.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 30069 {ECO:0000313|EMBL:KAJ5097320.1};
RA   Petersen C.;
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAJ5097320.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 30069 {ECO:0000313|EMBL:KAJ5097320.1};
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:KAJ5097320.1}.
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DR   EMBL; JAPQKH010000005; KAJ5097320.1; -; Genomic_DNA.
DR   OrthoDB; 9547406at2759; -.
DR   Proteomes; UP001149165; 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:UP001149165};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          87..128
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          350..513
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..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          951..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..290
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..969
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..998
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1015..1029
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1399 AA;  156019 MW;  36B69DE8807ACE97 CRC64;
     MAMAVEQPNG DSLAAGMVNS ASITPPHSAN GKKDVPEGVP SEFSDLELET KSASVQVEIP
     IKKEEKEDPV VEEEEVEPDH YYGDGKIPIF KPTMDQFRDF QAYINKIDKY GMKSGIVKVI
     PPKEWIDAQK PLDDQVKSIR VKNPIMQEFH GSHGTYTQAN IERQRSYNLP QWKGLCEESS
     HQPPARRGER RRNQERVNKV ASTPRPQPTP RPEGQKRRPG RPPKRTNQVK IKEEPIDETE
     NTKSEGPPTP VSPESHPVEA KSEDLSDGEP LPAAKPKGRQ PKSVTSRRKN NRGETVDHID
     ETVFESFDYR IHDNEDYTAE RCEELETAYW KSLMYNNPMY GADMPGSLFD ESTDVWNVAK
     LPNLLDVLGQ KVPGVNTAYL YLGMWKATFA WHLEDVDLYS INYIHFGAPK QWYSISQEDA
     PRFEAAMRSI WSSDAKSCDQ FLRHKTYLVS PSLLKSQYGI TVNRLVHYEG EFVITFPYGY
     HSGYNIGYNC AESVNFATER WMDYGRIAKK CHCEADSVWI DVDEIERKLR GEATPEYYGD
     YDSELEAFEG ASDLLTPPRS VPEKTSNRGR KRKLPGDGPR TKRPKLHPDG PRKLPCLLCP
     NNLDYEDLLP TEDGKGHAHR RCAGFIEETS ILRDPSGEEV VCDIDKIPKA RLGLKCLFCR
     EVYGACFQCN YGKCTRAYHA TCALLAGVQV EHGSLAVIAD DGNQYALPTV DLKCKFHRQK
     RPSGLLGESS DLDRRVIEAA RRQVQGDLIQ FQADKEINGA IVLQNRPEER TLLVKVLPRG
     DVIEMPYRWM LVVRKSNFVP LAVGIQALPA HLARKPEQRK DLEAAIPVAG TAFGDGQSPY
     QWAEFETVDA TRNQFAPPVK VHLGEAEQVW HYLGTQSTES RAQYTHNPSV PVHNPRANFL
     DSVKSLGVAG VSARALKISP HHHSHAATAP APPYKENLYA QHRPQIQYKH EPLSPANQTP
     HYQSRPPTSA ASLQHLAPPP HPAPAAGAAA AGPAMPSAFR TLPNQSARHA PYPSVTKSHV
     QQQHHLPSTN TFANVRELIA RRRLAQITDH ANVFAGYTIV SPELVVETLL GPMGSIPPAN
     GLEKLELAMA QQRVQPRAAD GTLLPPQTLN MRSEEVTRLL NMLRFSLVSH RERLDVIQKK
     ESEGVKLETI DRGSVAAAKM PGKYAFLDQQ RALAPNVYQS PYNMPSGLSE YAKTSYGLIP
     SPEEPPKASL ANDYFARLSP ELQEKIMKTC GSFVQRAIER SASHSRQSSA SNLRLSSVLA
     QQTENPTIDI TPVDDPPLTG LDMPLHADSP CSSFGRSHLR LQSPNEFPIH GPDPHPDHHD
     LFGDQQANTR FWQNGPWVAG DGNTPNEEHR PFFGPHERLK HDYASSDISL GKGPGSLHSV
     DMAGFGFDGP DDLIGGLSP
//
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