ID A0A9N9PKT3_9HELO Unreviewed; 1615 AA.
AC A0A9N9PKT3;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
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=HYFRA_00011481 {ECO:0000313|EMBL:CAG8957499.1};
OS Hymenoscyphus fraxineus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Hymenoscyphus.
OX NCBI_TaxID=746836 {ECO:0000313|EMBL:CAG8957499.1, ECO:0000313|Proteomes:UP000696280};
RN [1] {ECO:0000313|EMBL:CAG8957499.1}
RP NUCLEOTIDE SEQUENCE.
RA Durling M.;
RL Submitted (JUL-2021) 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:CAG8957499.1}.
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DR EMBL; CAJVRL010000079; CAG8957499.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000696280; 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:UP000696280};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 70..111
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 342..505
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 595..714
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1489..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..45
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..546
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1002
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1050
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1240
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1615 AA; 179254 MW; 1F69CAD88FAF1E2F CRC64;
MSAETMVAGP APGPAVEVNG LHSPPDSNTK DASDSELSDL DEEQPEQPAQ PKEEDDIGEI
EPAYYSNDGV PVFEPTMHQF KDFTIYMNKV NPYGMRSGIV KVIPPAEWKA AQPRLDEAVK
TIKVKEPIKQ DIMGTGGTYR QANMIHQRSY NLPQWRQLCE QSDHQPPAKR GERRANQDKP
VTRSTPRTKP SSNGNGSAPA GKRGRGRPSK SAATRAVTVE TDDAGQSTPD RLPTPVSPSA
RPDDNTESVK LEPDDDIETP EKPRLGSRQA KPTTVSVSSR RKNNRREREG KIDEAAFKDF
KYELEGNEFT PERCEELERA YWKTLTYAPP LYGADMPGTL FDDKTTSWNL GKLDNILDVM
GSKIPGVNTA YLYLGMWKAT FAWHLEDVDL YSINYVHFGA PKQWYAIAQG DARRFEAAMK
TIWPTDAKAC DQFLRHKTFL ISPSALLQNY NIKVNKIVAY PGEFVITFPY GYHSGYNLGY
NCAEAVNFGL ESWLEYGRVA KKCDCDQAQD SVWINVHELE RKLRGEETEY EETDEEEEDE
EEENENDIST LATPPLSTGG LKTKSEKKKR KRATNEKGGD SNIKRVKIRI KAATHEPCVL
CPNDIPSEAL LPTEDGQRAH QICAQYIPET SVDEGKAMDI KYIAKGRLEL KCNYCRSKKG
ACFQCSRKKC TRAYHATCAA AAGVLVEQGE IPVFGEDGTE YKEWGIEFSC RFHRVKREKK
LDSDALSDCE RLRKAGTEIK VGEVCQAQYL KGDIFAGVVV ENCKDEEVIL LDILPRGDRV
EVEYKWLLIP DPADYHLPKP SANALPMPKS RKDKASLNTS KRQADDIPRA EDPFVEGHTW
AEFNHEKIKL NPYQVKIDFT KENQIWFYLG KTSTEARAQY TEDPRIPRHN TKGNFLDTIP
KPVIAAPRQS YAASYPSNAK NSTPTPIRPP AKVLPAKTDR LEKPYVYKPR EQPRHETYGV
DAQAYRAQKD FLQRSVPQYS FGTDPRWASS TQPSKQSSSP TPFKANANST GHLPQISQVS
VAPPQYRNTQ SSMTPNQYSS TAQYATAASY NPAQHTSASQ HNSAQATSAV QHRPGSQHSA
AVQYSPTPKQ SPVVQQQASK VHSAAPTQYR STPPMATSKP NNPFGNRPQP QRPSNVFQKY
YYLQKEHNRS PSDYKSPYRP GGGFMNGYQG DLMEYTKATL FTGNRPGVST SQSNATPSYN
MSSSYNGTSH KPSPSLNSSQ SPSLDSYGPS PATPYSASPS LKPSMDNSGA SVIPPKTWEK
KKDSGQLHPA IRREFLHTIL NKQPTPLPQP SPTQSRSSVL QPPPLYERPP YPSTSYASQT
YTAPHNGYAA PSTPQNQVVP QPTYNKPVSL SASHPQQYSR PVAEASQKQQ SPQVPYAPPF
DYSGKAQGVT PTAAVPVAEH PRQQSSAGYH TPSTSYQTSS QLQASFSMHQ SATAKPQATQ
SPSAYTTAPA SNPPYGHAQH ATGVSTNHPQ PSYSQANYAA TSSIYERNTT SQVQASPVIP
PPLSNFRQSL PNTNSSLFQP AIKNTQAGSF HSPAPSHTTP ILPPPRQYQI QRQSEVQKST
YQHQQSFQRP DTQMTSSEQH LNAQPTSEPA DVPPDSCSIV EKMLRDLKKA RADSS
//
