ID A0A9P5BIY8_9HYPO Unreviewed; 1498 AA.
AC A0A9P5BIY8;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
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=FAGAP_1730 {ECO:0000313|EMBL:KAF4502053.1};
OS Fusarium agapanthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1803897 {ECO:0000313|EMBL:KAF4502053.1, ECO:0000313|Proteomes:UP000737391};
RN [1] {ECO:0000313|EMBL:KAF4502053.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 31653 {ECO:0000313|EMBL:KAF4502053.1};
RA Kim H.-S., Busman M., Brown D.W., Divon H., Uhlig S., Proctor R.H.;
RT "Identification and distribution of gene clusters putatively required for
RT synthesis of sphingolipid metabolism inhibitors in phylogenetically diverse
RT species of the filamentous fungus Fusarium.";
RL Submitted (JAN-2020) 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:KAF4502053.1}.
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DR EMBL; LUFC02000098; KAF4502053.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000737391; 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:UP000737391};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 116..157
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 394..557
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 640..763
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
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 215..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..240
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..263
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..596
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..958
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1207
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1286
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1313
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1435
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1498 AA; 167213 MW; 63263F7AC7BE4489 CRC64;
MSESTSTSID VGIAVAATPH SQDTVVATAR VDTNTKNSTT AQLSATFLHS PPDSNNTAKS
DGSDSELSDL EDEPILSDPP QPAPSSDSVN SDDMKEDADE DVDIGEVLPD SWSGAVPIFK
PTMHQFKDFK RFMEAVDSYG MKSGIIKVIP PQEWKDALPK LDDLVKQVKV REPIKQDIMG
FNGTYRQVNI LHGRSYNLPQ WRQLCDQSEH QPPARRGERR ANAEKPKART RAATATVAKP
SDPSIPKKRG RGRPAKRGGR GKRLKQEQAD DNEDRPMTPV SPKPEVAETE DKPVESVEKD
PGEEVEQDYE PTVGRMGGLR QARTKTQTVS ARRKYSRREG SAMIDEAAFK DWDYKMDISE
YTPERCEELE RAYWKTLTYA PPLYGADLMG TLFDESTEQW NLNKLPNLLD VLGEKVPGVN
TAYLYLGMWK ATFAWHLEDV DLYSINYLHF GAPKQWYSIS QADTRRFEAA MKNIWPTDAK
ACDQFLRHKG FLISPQHLKS HYNITVNKCV SYPGEFVVTY PYGYHSGYNL GYNCAEAVNF
ALDSWLDIGK FAKKCECAEA QDSVWINVYD IERKLRGEET EYEETEDEEE DDEDEQGGMP
TPPSGSGVKF RLAGRKRKRV PGEKGGKVKK IRLRLKSKAE PPCCLCPNDT PSADLLPTDD
CRKAHRLCAH YLPETYTETI DGQETVVNVS KIHKDRFELK CLYCRSKQGA CFQCSQKRCT
RAYHATCAAA AGVFVEEEEI PVFSEDGTEY KEQAFEFSCR YHRTKRDKKL DGDPLETDSR
VRTAASKLQP GETCQLQYFK GDIFAGVVVE NRHDEQTLLI DILPNGDRLE VEWKWLLVPD
PADYRLPKAS AKAIPMPASQ KAKEKLKTKR LHDGNPQKDD PFVEGCTWAE FNSHPVANKE
QVKIDFCKPD QIWYYLPKKS TEARAQFTED PRIPRHNPRG NFLSTVPKPV KPPRPVPGYP
SRQAYQPAVP YPAARLDKPY MYKPRTPAPN NYPAMGNFTT QRFTPAAPSP VPVQQQPGNY
RYPYARPMPA GQQATPAYSA QRFEVRQSPA YTPPGNTPGV QSPANTLPHY QQNQWQGRYT
PALPAPTPSH PEVAHPYPQP YQAPAPVNQH QASQASQARA ALQADVSIFQ KYPFFQVNHN
RDSTKYRTPY SPWGGFTNGY EGNFRAHIMA NKDAYLNGTI KHNRSQSNQN FGAYQPLHHH
PPGHGHRASP GSQPRISQQP NLKQVPTPSS GTGTPSFNQF PRPAIKQQYL PPMPMQTHVP
TQAQVQAPIQ PQVQPQAQPQ KSTPKPQQRP PQKPPQKAEE KPQQKLPQTT QPPNQSRVPK
IGAIFKEYKI PPKESPVPLP ANFLASMAPT SKIPAPIAAG KQQAESKGSP STPKAAKSIR
APQQTSSNGQ PMNSQKLGAK VSKTPIPIPR LPGVAQISSQ GSASASTRTQ QQGASPFQDS
KLTSTDSNLV HATDITAPAT STSSGQQDFA DVPGGESMEF MDRLMASIRT IARRDDAV
//
