ID A0AAD9W6D8_PHOAM Unreviewed; 1547 AA.
AC A0AAD9W6D8;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
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=N8I77_006234 {ECO:0000313|EMBL:KAK2607570.1};
OS Phomopsis amygdali (Fusicoccum amygdali).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214568 {ECO:0000313|EMBL:KAK2607570.1, ECO:0000313|Proteomes:UP001265746};
RN [1] {ECO:0000313|EMBL:KAK2607570.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DUCC20226 {ECO:0000313|EMBL:KAK2607570.1};
RA Noh H.;
RL Submitted (JUN-2023) 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:KAK2607570.1}.
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DR EMBL; JAUJFL010000003; KAK2607570.1; -; Genomic_DNA.
DR Proteomes; UP001265746; 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:UP001265746};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 134..175
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 425..588
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 680..803
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..74
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..115
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..270
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..634
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..657
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1291
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1380
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1547 AA; 170827 MW; F254A1E470CE2479 CRC64;
MSTEATGAAA PGTHNLNVNG NGTHGHDCDE STIAVVNPSA DTKSPKPTGL HSPPDSNNVD
ATDSELSDFD EAIADADSPP AITAIPRQTT PRPAPDDAPA SGDGSEPAQP EQAPTPEEDE
DIGEVLPDHW SGTVPVFRPT MDQFKDFKKF MRAVDSYGMK SGIIKIIPPE EWKNSLPDIS
ELVKTVRVRE PIKQDIMGSN GTYRQVNILH QRSYNLPQWR QLCDQSEHQP PARRGERRAN
ADKPKPATRS RAAATTNKSS TPAASSPARR TGGGRGRRGR GRGGARGKAK KSAAQEDTDI
EDRPMTPESP RPADDEKKGD AVVESIEQDP GVKVEDEDCE DEAPRRMGFS RQAKPKVQST
SARRKYSKRE GSAMIDEEAF KDWDYNMDIS DYTPERCEEL ERTYWKTLTY ATPLYGADLM
GTLFHEDTEM WNLNKLPNLL DVLGTKVPGV NTAYLYLGMW KATFAWHLED VDLYSINYLH
FGAPKQWYSI SQADARRFEA AMKSIWPTDA KACDQFLRHK AFLISPSHLL QHYNIKVNKC
LSYPGEFVVT YPYGYHSGYN LGYNCAEAVN FALDSWLPMG KIAKKCECAQ AQDSVWVDVY
EIERKLRGEP TPEYWTEEED EDDSDEDEDE DEEMGGLPSP PGSHTVRIKA PTRKRKQATI
SKDKKEKAKK LRLRVKAHVE PPCCLCPNDI PGAEILATDD GRKAHRLCAL YLPETYIETV
DGNETVFNVE NIEKARLELK CLYCRSKRGA CFQCSQKKCP RSYHATCAAA AGLFVEQGDV
PVFDKDGIEY KEEAFEFSCR FHRTKRDRRL DGDALEENTR IKEAARALKK NEIVQMQYYK
KEIFAGVVVE NRADEQTLLL DVIPNGARIE VEWKWLLLPD PEDFKLPKAS ANALPMPTSR
KAKEEINAKR SADEPPRAGD IFVEGPAPGK DFVWSEFHTC EASECKNKAQ TKIDFSKENQ
VWHYLGKTST EAKAQYTEDP RKPQHNPKCS FLDSVPKPPP PPRPQHQASY GATHPAQARA
PISTKPEKPY VYKPRKPVDT SFGPPFTTQK FAPSNTGAAG VPPLSFGTDP RFSAGLYSTN
KFAPVTANSP PQNQRHGSAQ FTPVPPPRQP QQHQQPQSIN PAWLSHTQVN SPQPQAIPFQ
APLSRQQSVP NVPAAMGQSS NFPMQQHAAP MQQPSQARAH VPQAFPQPAT PSVPQHAWQK
FSFFQAYHNR EPSRYRTPYA LWGGFTNGYE GDLRKHLMKK PESAPFSNRR LSFNLGGGLQ
GLTRPPSHRY SNSAGSSRSS PFSAPRARSQ SGAASPTSSF ASAMSPPPVP SRGHQRTPSV
PSTPSHPAMR PQYASSSQMN SNAGQTSQGN LAGSPNSLSN GMGLQGGSSS MEAQSSRASM
PPISPAGIPS QQPTFLNTSP QPIAHGASAA SPTLPMDVDP ETNESPAQQL KQQLRRISDP
KESPFRIPRS RGHTPRSSLN QLPRLQSPTE TADLSRQEER RASSGSTQAT TPSELAANGV
AVREFPEMAA DNKAFVEKMM LDLRRASQSA VDGTLNGLGE PTSATNP
//
