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
//