ID A0A8H6RAX8_9PEZI Unreviewed; 1378 AA.
AC A0A8H6RAX8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 13.
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=HII31_10933 {ECO:0000313|EMBL:KAF7187594.1};
OS Pseudocercospora fuligena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=685502 {ECO:0000313|EMBL:KAF7187594.1, ECO:0000313|Proteomes:UP000660729};
RN [1] {ECO:0000313|EMBL:KAF7187594.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PF001 {ECO:0000313|EMBL:KAF7187594.1};
RA Zaccaron A.;
RT "Draft genome resource of the tomato pathogen Pseudocercospora fuligena.";
RL Submitted (APR-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:KAF7187594.1}.
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DR EMBL; JABCIY010000224; KAF7187594.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000660729; 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:UP000660729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 73..114
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 328..491
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 571..694
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..216
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..529
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..987
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1117
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1233
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1344
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1378 AA; 154373 MW; 3EE04805965FE30C CRC64;
MATAGALSPE SHDAHEIKPT TEQTATVLTP PTSEDHERKH DGDESELSDL DLEEEEEEIF
PDHYWDEENG GRIPVFKPTM AQFADFQKFI GQIDKYGMKS GIVKVVPPQE WRESLPELHE
YVKRVKIKNP ITQEFNGTFG TYTQQNVEKQ RSYNLPEWKA LTEETSHQPP AKRGERRRGQ
KEVIRGGGSL RGRAAAIKEE DEGTPKPKRK PGRPRRNATP ADEASDDESV SSRKRAPATP
PAEPPAKKKP GRPAKNGGTK SVTSRRLNNT AETVDHIDEK AFKNFDYHLE DLDEFTPERC
AELESMYWKT MGFNQPMYAA DMPGSLFDDT VTSWNVAKLP NLLDVLGTKV PGVNTAYLYM
GMWKATFAWH LEDVDLYSIN YIHFGAPKQW YSISQEDARK FERAMKQAWP VDAKNCDQFL
RHKTYLISPD VLQKQYGVKV NKLVHYEGEF VITYPYGYHS GYNLGYNCAE SVNFATESWL
EFGRIAKKCN CESDNVWVDV GEIERKLRGE PTPEYYEETD SEGEDEEIED SKLPTPPASV
KGKGKKRKRE AKKEEPKKKK KIRIRIRLPT KEPCCMCPNE NKWEEVLPTD TGKQAHKSCA
LYTPETYIVN EDGKDKVYGV ANIDKARLDL KCNFCRSKKG ACFQCSSKKC TRAFHATCAV
AAGVLVDSGL VPTFSEDGTE YFEEGFDFRC RYHRPKMGKN PDTEAFEVNR LILDHAKQLK
PNDTVQARFV GGEVFGGLVV ENRPQERTVI VDVLPDGDRV EIEWRWICVL DPDDSVRPKP
SAAALPMPEN INKNKFSLEN RQDGVPSQDD TFNTDAAYKW HDFYNYHTPP PGFLTVPYKA
PLKLKVDVNA PDQLYYYLPE VSTDAKVFFT DKPGSKEIAP KGNFMDRVQP KHSTQYPAVK
QPLAPAQPAW RSQSFSNPAA LMNTAAGARN EKPYQYKPKE TVKPNVLCAV DYQALANQRS
FLAEGNRQSS VYSQQSPPPP MQQPPAPQYN YQGGDASRTA TPIRAFPSDQ YYSSKTLPAA
YQGEYSKFRR ESQGAQTMQR PNFEAAGYVP NYQSVSQQKT LLKQGPSSGS PIPPNPYTGP
YAPVSNSRPS SSAMSHHSPP IGGPLTPATT TSSLSKTDGP HADQAYLQNL QKYPYLLNSF
CRRPKVYESP YLIGGGFSAK ALEASQNGGS GDRRPRSMHT PSNSISALNE RRPSSQWTPP
SQVWSAAGLQ DKQQTPPPLP QNPLYQPGPP PRQYVPVQHS TPQDFQRQIQ QGGLASTASR
EGAQARMLRD QGYNNYSSYN PYPRNSFGNA YDTSRMWNSP QAPTPSPLSD PNTPGYGRGT
TPTASGPWGA LPQQQGGPLP NPLNHNGMNH RPQPGGPPGA GYGPMLPQMG GHETWRYH
//
