ID A0AAD9SVA4_9HELO Unreviewed; 1540 AA.
AC A0AAD9SVA4;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
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=QTJ16_006216 {ECO:0000313|EMBL:KAK2624266.1};
OS Diplocarpon rosae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Diplocarpon.
OX NCBI_TaxID=946125 {ECO:0000313|EMBL:KAK2624266.1, ECO:0000313|Proteomes:UP001285354};
RN [1] {ECO:0000313|EMBL:KAK2624266.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R4 {ECO:0000313|EMBL:KAK2624266.1};
RA Cheng Q.;
RT "Draft genome of Marssonina rosae.";
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:KAK2624266.1}.
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DR EMBL; JAUBYV010000010; KAK2624266.1; -; Genomic_DNA.
DR Proteomes; UP001285354; 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:UP001285354};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 59..100
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 321..484
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 572..694
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..186
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..200
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..540
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..551
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..907
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1133
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1280
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1305
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1372
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1395
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1501
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1540 AA; 171258 MW; E2BEA3F94DB45A06 CRC64;
MSTDTMAMPA AQPAPAGLNS PPDSMSAIKD GGSDSELSDL EPEVFALDVE PAYISEGNVP
VFQPTMDEFA DFTRYMTAIN KYGMRSGIVK VIPPPEWIAA QPRLDEAIKT IRVKEPIKQD
IMGTGGTYRQ ANIVHQRSYN LPQWRQLCEQ SEHQPPAKRG ERRANQDKQA RPAPKPKATG
KATTTGVKKR GAGRPPKNKS RSGTAEQDGT ITPDRLPTPV SPKLKAEEDN QPIKIEEDDY
DTPSKPKGGR QPKAISVSSR RKNNKRETGV VDEAAFKGFK YELEGEDFSK ERCDELERNY
WKTLTYAPPL YGADMPGTLF DERTTTWNLG KLDNILDVLG SKIPGVNTAY LYLGMWKATF
AWHLEDVDLY SINYVHFGAP KQWYSISQGD ARRFEAAMKT IWPTDAKACD QFLRHKTFLI
SPSQLASNFN IKVNKIVAHP GEFVITFPYG YHSGYNLGYN CAEAVNFGME SWLEYGRVAK
KCECSEAQDS VWIDVHEIDR KLRGEETEYE ETDYEEEEEE EESKSIDLLT PPESSGGSKP
KIPKKKRKRP TNNKDDKSNV KRIRVRIKGA SREPCILCPN DIPSEPLLFT EEGQRAHRKC
ALYIPETSIE TGEKETIVDV KYIDKARLEL KCNYCRSKKG ACFQCSQKKC TRAYHATCAA
AAGVFVEQGE IPVFGEDGTE YKEWGIEFSC RFHRTKREKK LDGDALGEDK RILKAGLELK
PGDVCQMQYY RGDIFAGAVV ENRTSEEMVL IDILPRGDRV EVEYKWLLIP DPADCHLQKP
SSKAIPMPKS FKDKESLNTT KRQADDLPRA DDLFVKGCTW AEFKSENISR NPAQVKVDFS
KENQIWFYLG KNSTDAKAQF TEDPAKPRHN PQGHFLDTIP KPAPAVPRKS YAASFPSKPN
PNVSSNSHTS NRPSQPTGKP SENFARPDKP YIYKPRNSGE MYSVDQKAYR DQQNFLQRST
PAPYAFGTDP RYRTAEALRP VNQCSAQNSS AVNDAQSRLG SMGSGARPVP AMNATRPGSG
EGSPPHSAYR LTAPAIPRPM NPFGSRPQSS STKPNPFAKY SYLQKEHNRS PLEYKSPYRP
GGGFMNGYQG SLQAHLQQTM FRPGGSTINI PSMPSLGGSS RSSNMGSQSA RSNNLRVSAN
NPNRTNGPVT SPGPAAVYSP KTIQTHPVAT PAKAAVNSWG KHGGSHLHPA IRQEYNAMYS
QQYQVPQPSS SSVLQPPAMY HRHATPLQAP HQPLSTPQSQ ARQYPQQPSQ PQLQNLHQAS
QRSQPRTSTT TTNSQATYRA IVPQSTTRPP NSQSQYQSSQ KARSSPANLP PAQQQYRPSP
STRNTQVRSP APQKLYQSSP MAPNSSANPP AAQQQQTEAI PAAAASPMDS PAFQQQRKSA
AYSPTSQQQN PTSQSITNAL DRPHVSQPQY QLSPAVSKAQ IQPHGSDQHY QPSLDTVTPV
SEPQYQPLSA ANNLQQPSAH KMTSQAQYQQ ASRASTQESK PVYPHQQYFQ QQQAQPQQYH
PLPMPPLGQD SPVRDPPDVP ADSTRLVERM MMTLKRAPAA
//
