ID A0A9W9F131_9EURO Unreviewed; 1389 AA.
AC A0A9W9F131;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 9.
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=NUU61_006532 {ECO:0000313|EMBL:KAJ5091662.1};
OS Penicillium alfredii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1506179 {ECO:0000313|EMBL:KAJ5091662.1, ECO:0000313|Proteomes:UP001141434};
RN [1] {ECO:0000313|EMBL:KAJ5091662.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 34128 {ECO:0000313|EMBL:KAJ5091662.1};
RA Petersen C.;
RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAJ5091662.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 34128 {ECO:0000313|EMBL:KAJ5091662.1};
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:KAJ5091662.1}.
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DR EMBL; JAPMSZ010000009; KAJ5091662.1; -; Genomic_DNA.
DR RefSeq; XP_056509860.1; XM_056657060.1.
DR GeneID; 81396229; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP001141434; 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:UP001141434};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 82..123
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 345..508
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 587..712
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..285
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..987
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1389 AA; 154448 MW; 47CA60C7EC42512A CRC64;
MAAILDQPHL DPVAAGPVDS ASITPPQSAN GKKDAPEGVP SELSDLELDS KTAAPPDAIS
AKQEIEEEEE IEPDHYYGGG KIPVFKPTMD QFRDFQSFIN RIDKYGMQAG IVKVVPPKEW
SESLPALDDA VKNIRVKNPI MQEFHGSHGT YTQANMERQR SYNLPQWKGL CEESSHQPPA
RRGERRRNQE RANRAAHTPR PQPVRPDGQK RRPGRPPKRA NQVKVKEEPP ADDVDKSKLE
GPPTPVSPES NPVEAKSEDL SDGESLPATK PKAKQPKSVN ARRKNNRGDA VDYVDEEAFN
GFDYRIHDNE DYTAERCDEL ETAYWKSLMF NNPMYGADMP GSLFEESTAS WNVAKLPNLL
DVLGQKVPGV NTAYLYLGMW KATFAWHLED VDLYSINYIH FGAPKQWYSI SQEDAPRFEQ
AMRTIWSSDA KNCNQFLRHK TYLVSPSLLK SQFGITVNRL VHYEGEFVIT FPYGYHSGYN
IGYNCAESVN FATEKWLDYG RIAKKCHCEA DSVWIDVDEI ERKLRGETTP EYYGEFESEF
DGFEGASDLL TPPRSVPEKS SRGRKRKHPD DGPRTKRPRL HPEGPRKIPC LLCPNNLDYE
DLLPTEDGKG HVHRRCASFI EETIILRDAS GTEVVCDIDK IPKARLGLKC LFCREVRGAC
FQCNFGKCTR AYHPTCALLA GVQVEHGSIA VIADDGAQYS IPSVDLKCKF HRQKRQAGLL
GESSDLDRRV IETARRLVQG DLIQFQADKE INGAIVLQNR PEERALLLKV LPRGDVIEMP
YRWMLVVRKS NFVPLAPGIQ PLPTHLMRKP DQRKELESAV PVAGSAFGDS RSPYQWAEFE
TVDATNRQFA PPVTVSLDKG EQMWHYLGAQ STESRAQYTH NPSVPVHNPR ANFLDSVKSL
GVAGVSARAS KISPHHFHYA TAPAPPYQQN LYAQHRPHLQ HKSSAVNAPH LQSRPPFSAA
SLQHLAPPPP PTSAGAAAAG APAMPSAFRT LSNQSARHAP YPSVAKSHAQ QQHHLPATNT
FANVRELIAR RRLAQITDHA NVFAGYTIVS PELVVETLLG PMGSIPPANG LEKLELAMAQ
QRVQPRAADG TLLPPQTLNM RSEEVTRLLQ MLRFSLVSHR ERLDVIQKKE SEGVKQETVD
RGSIAAAKVP GKYAFLDQQR AQAPNVYQSP YNMPSGLSEY AKTTYGLIPS PETPPKPSLA
NDYFASLSPK DQEKILKTCG SFVQRAFERS ASHSRHSSSA SNLRLSSALA QQTENPTIDI
TTVEDPPLTG LDLPLHADSP CSSFGRSHLR FHSPNDFPIH GPDPHPDHHD LFGDQQANTR
FWQNGPWAAG DGNTPNDETR PFFGPHERLK HDYASSDISL GKGPGSLHSV DMAGFGLDGT
EDLCAELSP
//
