ID A0A0F4ZFR3_9PEZI Unreviewed; 1172 AA.
AC A0A0F4ZFR3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 02-APR-2025, entry version 32.
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=TD95_001946 {ECO:0000313|EMBL:KKA29352.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA29352.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA29352.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA29352.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-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:KKA29352.1}.
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DR EMBL; LAEV01000882; KKA29352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZFR3; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000033483; 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:UP000033483};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 108..149
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 398..561
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 649..773
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..251
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..972
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1172 AA; 130264 MW; A6E2B087BD086D3E CRC64;
MDPSADAPAA SPMLTGPATN LQNSGPRTRR RASLAAAAAA AVTQEKKPAQ DDSDLSSCDA
DAQGDQTFAT AETSIQAPET GCEIDPEKQA AEDEDIGEVL PAEWSGKVPI FRPTMQQFKD
FKKFMEAVDK YGMTSGIIKI VPPAEWKQSL PPIDHLVKQV RVRNPIKQDI MGSSGTYRQV
NFVHGRIYNV PQWRALCDQS EHQPPARRGE RRANADRPRS APSAAPAPRP ARTESSTFGR
KKRRRRGRQP MRRTAVDDDE EDHQNQHHER PMTPISADDD DGDDDALHTE KTPHTRHSKT
LDNHEPIASI EDTPAPPRSG RMRAVKEEKT QSTSARRKYC RREASAKVDE EAFRNFDYHM
DISDFTPERC EELERIYWKT LTYAPPLYGA DLMGTLFDES TELWNLNKLP NLLDVLGTKV
PGVNTAYLYL GMWKATFAWH LEDVDLYSIN YLHFGAPKQW YSISQADARR FEAAMKTIWP
QEAKSCDQFL RHKGFLISPQ HLKNHFNITV NKVLSYPGEF VVTYPYGYHS GYNLGYNCAE
AVNFALDTWL PMGKIAKKCE CAEAQDSVWV DVYEIERKLR GEEEEYEYVE MEVDDDDDDN
TGHGIPSPPD SSNDKTGLKR KRGPQAGSNR WTKKLRTVRV AVKSKARADP VCCLCPNDVR
GLEILPTDDG RTAHRMCARY LPETYFDEAA DGSEVVCGVD AVMAARHDLK CLFCHSKRGA
CIQCSQSSCS RVYHASCAAA SGAFVEEAEV PVFGADGTEY KDEAFEVTCR FHRVRRDRGV
TGYDLENNVR VSRAAAALKP GDICQLQLHT KDVFAGVVLE NRCDEEMLVV ESMPNRDLVE
VQWKWLVVAD AADFHLPRAS AAAVALPRSK AARDALCAVR GDGAAPRRDE PFVDGYTWAE
FVANRDTAEW VQAPAVEFGT GKTMLWMYLG AESTDSRALY THDWAVQRAD AAADFLASVP
RRRQKRETKR QQRQQQQQPV FVPQGGLMPR LAPVGGYPAY YPVHQQQVLP QQFSQQQQQQ
PTYYGLAIPG YSGAIAHSQD QQQLGLPKKG VLPVCAPIPV KQTPVPIPAK YLAASTMHKP
SPPPAAAAAA ASCGGGAVSV SAAPGTSKTP LRKSTTPIPI PRILGMQQQQ QQQPLAEKDG
EDVALAEVPP ESMVLVNNVI LSLRRESQDG AF
//
