ID A0A8H5UV26_9HYPO Unreviewed; 1495 AA.
AC A0A8H5UV26;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
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=FPCIR_2992 {ECO:0000313|EMBL:KAF5598429.1};
OS Fusarium pseudocircinatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=56676 {ECO:0000313|EMBL:KAF5598429.1, ECO:0000313|Proteomes:UP000546213};
RN [1] {ECO:0000313|EMBL:KAF5598429.1, ECO:0000313|Proteomes:UP000546213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 36939 {ECO:0000313|EMBL:KAF5598429.1,
RC ECO:0000313|Proteomes:UP000546213};
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 (MAY-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:KAF5598429.1}.
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DR EMBL; JAAOAS010000061; KAF5598429.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000546213; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:KAF5598429.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000546213};
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..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..310
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..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..43
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 246..263
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..276
FT /note="Basic and acidic 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..960
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1286
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1315
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1495 AA; 166819 MW; 05A93031E8776A38 CRC64;
MSESTSTSID AGIAVAATPH SQDTVVATAP VDTNTKNTST AQPDATFLHS PPDSNNTAKS
DGSDSELSDL EDEPILSDPP QPVHSSDNVN SDDKKEDAEE DIDIGEVLPD SWSGAVPIFR
PTMHQFKDFK RFMEAIDSYG MKSGIIKVIP PQEWKDALPK LDDLVKQVKV REPIKQDIMG
SNGTYRQVNI LHGRSYNLPQ WRQLCDQSEH QPPARRGERR ANAEKPKPRT RAATATVAKP
PDPSTPKKRG RGRPAKRGGR GKRLKQEQAD NNEDRPMTPV SPKPEVAETE DKPVESVEKD
PGEEVEEDYE PTVGRMGGLR QARTKTQTVS ARRKYSRREG SAMIDEAAFK DWDYKMDISE
YTPERCEELE RAYWKTLTYA PPLYGADLMG TLFDESTEQW NLNKLPNLLD VLGEKVPGVN
TAYLYLGMWK ATFAWHLEDV DLYSINYLHF GAPKQWYSIS QADARRFEAA MKNIWPTDAK
ACDQFLRHKG FLISPQHLKS HYNITVNKCV SYPGEFVVTY PYGYHSGYNL GYNCAEAVNF
ALDSWLDIGK IAKKCECAEA QDSVWINVYD IERKLRGEET EYEETEDEEE DDDDEQGGMP
TPPSGSGVKF RLAGRKRKRV PGEKGGKVKK IRLRLKSKVE PPCCLCPNDT PSADLLPTDD
GRKAHRLCAH YLPETYTETI DGQETVVNVS KIHKDRFELK CLYCRSKQGA CFQCSQKRCA
RAYHATCAAA AGVFVEEEEI PVFGEDGTEY KEQAFEFSCR YHRTKRDKKL DGDALETDSR
VRTAASKLQP GETCQLQHFK GDIFAGVVVE NRHDEQTLLI DILPNGDRLE VEWKWLLVPD
PADYRLPKAS SKAIPMPASQ KAKEKLKTKR LHDGKPQKDD PFVEGCTWAE FNSHPVANKD
QVKIDFCKPD QVWYYLPKKS TEARAQFTED PRIPRHNPRG NFLSTVPKPV KPPRPVPVYP
PQQAYQPAVP YPTARLDKPY MYKPRTPASH NYPAMGNFTT QRFTPAAPSP VQQQPGSYRY
PYAQSISVGQ QAAPAYSAQR FEVRRSPAYT PPGNTPRIQS PANTLSHYQQ DQWHRRHTAA
LPAPTPSHPG VAHPYPQPYQ APAPVNHQAS QARVAPQADV SIFQKYPFFQ VNHNRDSTKY
RTPYSPWGGF TNGYEGNFRA HIMANKDAYL NGTIKDNRFQ SNQNFGAYQP PHHQPPGHSH
HASPGSQPRI SQQPNLKQVP TPASGTRTPS FSQFPRPAIK QQYLPPMPMQ TQAPVPASAQ
VQAPIQAQAP PQAQPQKSTP KAQQKPPQKP PQKAEEKPQQ NPPQTTQPPN QSSKPKIGTI
FKEYKIPPKE SPVPLPANFL ASMAPTSKTP APVASGKPIL QQAEGKGSPC TPKAAKPIRE
AQQTLSNGQP MNNQKFGTKV SKTPIPFPRL PGLAQFSSQG SASAPTQQQG ASPSQDSKLK
CTDSNLVHAT DTTVPATNTA SGQQDFADVP GGESMEFMDR LMASIRTIAH RDNAV
//
