ID A0A1B8B4M0_FUSPO Unreviewed; 1513 AA.
AC A0A1B8B4M0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=FPOA_01601 {ECO:0000313|EMBL:OBS27659.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS27659.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS27659.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS27659.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; 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:ARBA00000040};
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:OBS27659.1}.
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DR EMBL; LYXU01000001; OBS27659.1; -; Genomic_DNA.
DR STRING; 36050.A0A1B8B4M0; -.
DR OMA; PWGGFTN; -.
DR Proteomes; UP000091967; Unassembled WGS sequence.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 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; 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; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 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:UP000091967};
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 644..767
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..112
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 575..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..599
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..631
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1222
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1513 AA; 169071 MW; 3A53E7AE6F1DE727 CRC64;
MSESTSKSID AGAAVANAPD SRDPVVATAP ADSNPNNTAT AKTDPAFLHS PPDSNNTAKS
DGSDSELSDL EDEPILSDPP QPVDPSDKNT SDEDKDKPSH EDIGEVLPDD WSGAVPIFKP
TMHQFRDFKR FMEAVNSYGM KSGIIKVIPP QEWIDSLPKL DDLVKQVKVR EPIKQDIMGS
NGTYRQVNIV HGRSYNLPQW RQLCDQSEHQ PPARRGERRA NAEKPKPRTR TTAPAPKPVD
PSVPKKRGRG RPAKRGGRGR RANPEPAEDA EDRPMTPISP KPDATEMDDK PVESVEQDPG
EEVEDDYEPK VGRMGVSRPA RTKTQTVSAR RKYSRREGSA MIDEAAFKDW DYKMEISEYT
PERCEELERA YWKTLTYAPP LYGADLMGTL FDESTEEWNL NKLPNLLDVL GTKVPGVNTA
YLYLGMWKAT FAWHLEDVDL YSINYLHFGA PKQWYSISQA DARRFEAAMK NIWPTDAKAC
DQFLRHKGFL ISPQHLKSHY NITVNKVVSY PGEFVVTYPY GYHSGYNLGY NCAEAVNFAL
DSWLEIGKIA KKCECAQAQD SVWVNVYEIE RKLRGEETEY EETEEEEEDD EEDDDDEQSG
MPTPPSISGV KIKEPRRKRK RGPGDKSGKV KVKKIRLRLK AKAEPPCCLC PNDTPSADLL
PTDDGRKAHR LCAHYLPETY IETIDNQETV VNVSEIQKDR LDLKCLYCRS KRGACFQCSQ
KKCARAYHAT CAAAAGVFVE EEEVPVFGED GTEYKEQAFE FSCRFHRTKR DKKLDGELLE
MDTRIQTSAS KIQPGETCQF QYHKGDIFAG VVIENRADEQ TLLVDILPNG DRLEVQWKWL
LVPDPADYRL PKASANAIPM PASQKAKDKL KTRRFHDGKP QKDDPFVEGC TWAEFQLHPV
SNKEQVNIDF SKPDQIWHYL PKTSTDARAQ FTEDPAKQRH NPQGNFLSTV PKPVKPVRPP
RAVPPYAQQR PYQPGTPYNT GRLERPYVYK PRIPAESNLP TMGSFTTQRF APTAPLPVPI
QHHHTQYPSY AQPVPPGHQS PHPAYSAQRF EVRSSPAPIP PGSTPTMHNP LNAPVHSQHT
QWPRVTNASH PSPVPAPAAG VTYFHNGAHQ SPYQAPAHHQ QAHPVQQQNH HMKASWQVHQ
SIYQRYPFFQ VNYNRDSNKY RTPYATQGGF TNGYEGNMRA HIMANPDAFL RGQPSNYNHG
AHSSPYQRPS AVPPPAPSPS QMPPSGHEFR QQSFPKGVPA PSPMPTHPTS GQFPRPALKA
QYLPPIQSQT QAQGHPQQCQ QPQQPQPNPQ QMRNPQDTTQ TPNQNSKLKT ATVFKPYKIP
PKESPVPLPA NFLAAMTSTP NTMAAAGQLA LQQPSNKGSP VEPKPVRKVQ ATQQSPSGAS
TPGKQPLGAK ISETPVPIPR LPGFVPVSTS REQAASPQTH VLNHNQSSRL LPSHQGSPVT
PVATKEQMTP SVRDGKLALT NVNPGNAPQT VLAEQANLFQ PHDFPDVPGS GSMKFMDSLL
ENIRTIARRD EKP
//
