ID A0A2L2T6P2_9HYPO Unreviewed; 1512 AA.
AC A0A2L2T6P2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
OS Fusarium venenatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI65369.1, ECO:0000313|Proteomes:UP000245910};
RN [1] {ECO:0000313|Proteomes:UP000245910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA King R.;
RL Submitted (OCT-2014) 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}.
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DR EMBL; LN649229; CEI65369.1; -; Genomic_DNA.
DR RefSeq; XP_025589089.1; XM_025729911.2.
DR STRING; 56646.A0A2L2T6P2; -.
DR GeneID; 37253525; -.
DR KEGG; fvn:FVRRES_01881; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000245910; Chromosome I.
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:UP000245910};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 115..156
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 392..555
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 643..766
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..261
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..307
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..598
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1290
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 169010 MW; 28B446DA15004D3C CRC64;
MSESTSKSID AGAAVANTTD SRDPVVATAP VDSNPNNTAT AKTDPAFLHS PPDSNNMAKS
DGSDSELSDL EDEPILSDPP QPLDSSDKNT SDEDKDKPSD EDIGEVLPDH WSGAVPIFKP
TMHQFRDFKR FMEAVDSYGM KSGIIKIIPP QEWKDSLPKL DNLVKQVKVR EPIKQDIMGS
NGTYRQVNIV HGRSYNLPQW RQLCDQSEHQ PPARRGERRA NAEKPKPRTQ KAAPASKPVD
PSVPKKRGRG RPAKRGGRGR RANPEPAEDA EDRPMTPVSP KPDATEMEDK PVESVEQDPG
EEVEDDYEPK VGRMGISRPA RTKTQTVSAR RKYSRREGSA MVDEAAFKDW DYKMDTSEYT
PERCEELERA YWKTLTYAPP LYGADLMGTL FDESTEQWNL NKLPNLLDVL GTKVPGVNTA
YLYLGMWKAT FAWHLEDVDL YSINYLHFGA PKQWYSISQA DARRFEAAMK NIWPTDAKAC
DQFLRHKGFL ISPQHLKSHY NITVNKVVSY PGEFVVTYPY GYHSGYNLGY NCAEAVNFAL
DSWLEIGKIA KKCECAQAQD SVWVNVYEIE RKLRGEETEH EETEEEEEDD EEEDDDESGM
PTPPSTSGVK IKEPRRKRKR GPGDKSGKVK VKKIRLRLKT KAEPPCCLCP NDTPSAELLP
TDDGRKAHRL CAHYLPETYI ETIDNQETVV NVSEIHKDRL DLKCLYCRSK RGACFQCSQK
KCARAYHATC AAAAGVFVEE EEVPVFGEDG TEYKEQAFEF SCRFHRTKRD KKLDGELLET
DTRVKTSASK IQPGETCQFQ YYKGDIFAGV VIENRADEQT LLVDILPNGD RLEVQWKWLL
VPNPADYRLP KASANAIPMP ASQKAKDKLK TKRLHDGKPQ KDDPFVEGCT WAEFQLHPVS
NKDQVNIDFS KPDQIWHYLP KTSTDARAQF TEDPTKQRHN PQGNFLSTVP KLLKPVRPPR
AVPPYAQQRP YQPGTPYNAG RLDRPYVYKP RIPAEINLPT MGSFTTQRFA PAAPLPAPNQ
HHTQYPSYAQ PAPPGHQSPH PAYSAQRFEV RSSPAHTPPG STPTMHSPMK VPVHPQQTQW
PRVTNVSHPP TPAPAAGVMY PHNGAHQSPY QASAHYQQAH PVQQQNHHMK ASWQVHQSIY
QKYPFFQVNY NRDSSKYRTP YAAWGGFTNG YEGNFRAHIM ANQDAFLRGQ PSNHNYGAHS
SPHQQPSAVP PPASSPSQMP PSGFDFRQQS FPKGVPAPSP SPMPTHPTSG QFSRPALKAQ
YLPPIQAQAQ AQGHAQQHQQ PQPSQPNPQQ VRKPQETTKT PNQNSKPKTA TVFKPYKIPP
KESPVPLPAN FLAAMTSTPN TVAAAVGQPA LQQSSNKGSP VEPKPVRKVQ ATQQSPSGAY
TPGKQPLGAK ISETPVPIPR LPGFMPVSTS REVASPQKYV LNQVHSNRHL PSHQGSLVTP
VAAQEQVASS VRDGKLVLTN TNPENAPQTV LAEQAIPFQP QDFPDVPGSE SMKFMDSLLE
NIRTIVRRDE KP
//
