ID A0A9P7AWJ1_9HELO Unreviewed; 1371 AA.
AC A0A9P7AWJ1;
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=D0Z07_6004 {ECO:0000313|EMBL:KAG0648180.1};
OS Hyphodiscus hymeniophilus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyphodiscaceae; Hyphodiscus.
OX NCBI_TaxID=353542 {ECO:0000313|EMBL:KAG0648180.1, ECO:0000313|Proteomes:UP000785200};
RN [1] {ECO:0000313|EMBL:KAG0648180.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 34498 {ECO:0000313|EMBL:KAG0648180.1};
RA Kramer G., Nodwell J.;
RT "Hyphodiscus hymeniophilus genome sequencing and assembly.";
RL Submitted (JUL-2019) 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:KAG0648180.1}.
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DR EMBL; VNKQ01000011; KAG0648180.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000785200; 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:UP000785200};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 63..104
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 322..485
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 574..696
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..199
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..525
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1011
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1036
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1063
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1177
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1193
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1269
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1371 AA; 154118 MW; 503A70E6DD95542F CRC64;
MSIDAMAVPA LGAEAQLQSP PESNKDSPHS HNVDGSDSEL SDLEEEEEDI GTVVPDHYSD
DGVPVFKPSM DQFKSFKLYM SKINAYGMKS GIVKVIPPPE WRADLPRLDE AIKTVRVKEP
IKQDIMGTSG TYRQANILHQ RSYNLPQWRQ LCEQSEHQPP AKRGERRANQ DKAPKPKSRG
TSTPTLGGKR KGRLSKPKSK ATNLAEDGTS TPDRLPTPDS PSTKPEVDME SVKQEMDDED
EIQSRPKGGR QPKSISVSSR RKYNRREAAA KVDEEAFKDF KYELENSDYS KERCEELERA
YWKTLTYAPP LYGADMPGTL FDDRTTTWNL GKLENLLDIL GTKIPGVNTA YLYLGMWKAT
FAWHLEDVDL YSINYLHFGA PKQWYSISQG DARRFEAAMK SIWPTDAKAC DQFLRHKTFL
ISPSHLLQNF NIKVNKIVHH PGEFVITFPY GYHSGYNLGY NCAEAVNFAL DSWMEYGRVA
KKCDCSEAQD SVWIDIREIE RKLRGEETDY EETDEEEDED EDENGPTDLP TPPESSGDIK
PKAPKRKRKR PINDKGNDNS NVKRIRVRIK APSKEPCILC PNDIPSEPLL PTEDGQKAHR
LCALYIPETS IDSEETEKVV DIKYINKARL DLKCNYCRSK KGACFQCSQK KCTRAYHATC
AAAAGVLVEQ GEIPVFGEDG TEYKDWGIEF SCRFHRSKRD KKLDSDALGD SDRIRKAASE
LKMGQTCQVQ FYRADIFAGA VVENRKSEEM LLLDILPRGD RVEVEYKWLL IPDPADFRLA
KPSATAIPMP KSRSAKESLN TTKRLADDAP RADDKFGEGF TWSEFKCEKI ARNPFQLKID
FGKEDQIWFY LGRNSTEAKA QFTEDLSKPR HNPKGHFLDT IPKPVISAPR QSYGASYPST
NINQNALNAS RTSNASRPQT AAPVSISFKP QKPYVYKPRD DSESYRIDPQ AYRQQQSFLQ
RSAPYNFGTD PRFRASDSPM TPATPYPKYS STTPQPQSLT QPQLPQQANQ QMGTQAYQSH
MPQQVHQHQL PQQVLQPPRP TLSQSPLAPP PGYHRPPYTP PTYVPAIQST KPSNNVVQPP
KPNNPFSGRS QSTRPNPFAK PGGGFMNGYQ GDTEKHLQQT LFKNRSSSIG SLSNPPPSFA
GNSRLYSPNP SSTGQSYIAT TPSSSGSHSM SKQQAPITLP PSTLPPVPRP APNPAAHSTW
EKKDHSQLHP AIRQDYNSMF NNQYQTPPLA SFSTANSQTQ SPHQSALAPP PPYYQQQYQQ
APPASLASPR NPSFAQPAQL YQQPGKSQPY QPQYHSHKQP HHQESKPVYA HQQYFQKPQP
QAPAIQMPQS QSQVEAQARA YGVFPDVPAD STSLIERMMK NLKKATSTST P
//
