ID A0A225ARW1_TALAT Unreviewed; 1367 AA.
AC A0A225ARW1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-OCT-2025, entry version 25.
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=UA08_00748 {ECO:0000313|EMBL:OKL64312.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL64312.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL64312.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL64312.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:OKL64312.1}.
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DR EMBL; LFMY01000001; OKL64312.1; -; Genomic_DNA.
DR RefSeq; XP_020124433.1; XM_020260588.1.
DR STRING; 1441469.A0A225ARW1; -.
DR GeneID; 31000503; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000214365; 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:UP000214365};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 74..115
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 337..500
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 581..706
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..278
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..931
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1367 AA; 153728 MW; BFF5DF57CEC924CF CRC64;
MANAENQKAS ALNSLHSVET NITPPNSADG KKNASEGVPS ELSDLDLDHN AAAPSVEAVE
QDIEPDYFYE GGRIPVFKPT MDQFRDFQAY VQKIDKYGMK SGIVKVIPPQ EWRDSLPALD
EAVKSIRVKN PIMQEFHGAH GTYTQANIEK QRSYNLPQWK ALCEDGSHQP PARRGERRRN
QEKVPRPAIV KSQTVRSTSQ KRGPGRPPKR AKEPKIKEES PAEDRSERSR LEGPPTPVSP
ESNPIETKTE DLSDGEELPA AKRKGRQPKS VSSRRKHNHG EAMDQIDEEA FKDFDYRIHD
NDEYTAERCD ELETAYWKSL MFNNPMYGAD MPGSLFDEST TSWNVAKLPN LLDVLGQKVP
GVNTAYLYLG MWKATFAWHL EDVDLYSINY IHFGAPKQWY SISQEDAPRF EAAMKSFWPS
DAKNCDQFLR HKTYLVSPSI LKSRFGISVN KVVHYEGEFM ITYPYGYHSG FNLGYNCAES
VNFATEKWLD YGRMAKKCNC ESDSVWIDIA DIERKLRGEP TPNYYDDDDI DSYLSELDGA
SDLLTPPRSV PEKSGRGRKR KLEGGEPRSK RVRIQNHDVR KIPCVLCPND MDYEDLLPTE
DGKSHAHRRC ATYIEETTIL RDESGREVVC DIDRIPKARL GLKCLFCREV RGACFQCNFG
NCTRAYHPTC ALLAGVQVEF GSILVIADSG QQYYVPSVDL KCKYHRQKRL GPSETPDESR
KVLQAASRLS MGDLLQFQAD KEINGAIVLE NRPVERMLRL KVLPRGDILE LPYRWILVVR
KTNFAPLPPG TQPLPAHLVR KAETRRDPSG TAPLPGTPFG DANARFQWAE FEAAPLPREA
IGVPVDIAGG RAEQLWYYLG ESSTECRAQF THNPSVTVHN PRSNFLESAK ASAGRFRLPP
SSSGTAPPHH LHAPPNTTLP RSSSSLQRRS PNTAMTPAYR HLPHHHTTNA NSTAHFFPAN
AVRANPYAGF QKPQPDPPTN TFANVRELIA RRRLAQITEH ANVFAGYRIV SPELVVETLL
GPMGSVPPPN AMEKLELAMA QQRVQPRALD GTLLPPQPLN MRSEEVTRLL QMLRFSIVSH
RERLDVIPKR ESDYPKQEPF DRPNYAAGRV AGRYAYLEQQ QAQTPTVYRS PYESPFGVSE
WAKKEYNLVE EEPASKPSLA NDYFASLSPA DQEKIVKACG SWVQERIVER PPSHSRQSST
SNFRLSTVLA QQNDNPTIDI TAVDDLPMNG MDRLDRLDRL DFPLHADSPA SSFSRPHLVG
FPSPHDFNSH GDHDSSIVPR HLSDHHDLFG DQQANTRFWQ HGPWAPAGDG TTPIEENRPF
FGPHERLKHD YASSELSLGR GPGSLHSVDM AGFGMDTTED LCDALSP
//
