ID A0A9W8XFE6_9PLEO Unreviewed; 1403 AA.
AC A0A9W8XFE6;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
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=N0V89_009365 {ECO:0000313|EMBL:KAJ4347993.1};
OS Didymosphaeria variabile.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Didymosphaeria.
OX NCBI_TaxID=1932322 {ECO:0000313|EMBL:KAJ4347993.1, ECO:0000313|Proteomes:UP001140513};
RN [1] {ECO:0000313|EMBL:KAJ4347993.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IMI 356815 {ECO:0000313|EMBL:KAJ4347993.1};
RA Hill R.;
RT "Tapping the CABI collections for fungal endophytes: first genome
RT assemblies for Collariella, Neodidymelliopsis, Ascochyta clinopodiicola,
RT Didymella pomorum, Didymosphaeria variabile, Neocosmospora piperis and
RT Neocucurbitaria cava.";
RL Submitted (OCT-2022) 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:KAJ4347993.1}.
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DR EMBL; JAPEUX010000007; KAJ4347993.1; -; Genomic_DNA.
DR RefSeq; XP_056067381.1; XM_056218116.1.
DR GeneID; 80912895; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP001140513; 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 FunFam; 3.30.40.10:FF:000377; 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:UP001140513};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 78..119
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 355..518
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 609..732
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..20
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..68
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..223
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..280
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..554
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..584
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..977
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1403 AA; 156264 MW; A2C967D069B53D03 CRC64;
MEAPAPAPVS APAEVVPSVE NPTHDDKHED LANKPALTPP TSEDMDKRDE RMSSELSELD
SDDGEDIEPD HYWDGGKIPV FKPTMDQFRN FKRFIDKIDK YGMKSGIVKV IPPTEWRDSL
PDLSEAVKTI KVKNPITQEF AGQHGIYTQA NIEKQRSYNL PEWKAVTEEA HHQPPVRRGE
RRRAAAEAPS RNRSTRAQTN TANADGASPA PKRGPGRPRR GRAAKKEEVD DEDTASIDVP
PTPKSPGPEE DKKTSVKKIK EEELDESPVR SRGRQPRGRQ PRGDTKKSTA SRRMNNRTAM
ADYVDEAAFE DFDYHLDNVS EFSADRCKEL EENYWKTVNF GQPMYGADMP GSLFDERTTS
WNVAKLPNLL DVLGTKVPGV NTAYLYLGMW KATFAWHLED VDLYSINYIH FGAPKQWYSI
SQADARKFEA AMKQIWPNDA KNCSQFLRHK TYLISPEKLE KNFGIKVNRL VHYEGEFVIT
YPYGYHSGYN IGYNCAESVN FANESWLSYG RIAKKCLCES DSVWVDVNEI ERKLRGEPTP
EYIEETDSEG EDEIDHLPSP PPSVAGKARS KPGRKPAGNK RKRGNKEPEE APKRKVRRIR
IRIKVPGRGM PCILCPNDVE YDELLPTDNG MKAHRICADY TPETYILQKN GVETICNVAN
IGKDRLELKC NYCRSKRGAV FQCSQKKCTR AFHATCAMAA GVQVDLGPMP TFDEEGTEYY
YDGYDFRCRF HRPKKRNNKT VDVDYLEKDK FIMNYAKGLK PKDAIQFQYV GGEMYQIYGG
LVVENRPGEQ ALLVDVLPDG DRVEVEWKYI LKLAPEDSQR PKPSANAKPL PDHLKENDAS
LDISNRTDGV PEMGDPFHDP NSDQKWAEFN TAEAVIQKVA KVDFSKPNHV WFYLGKNSTE
ARPQYTHDLS KRVHNPKSNF LDTVKPPPPV IPHYQYQQRS YPASYPIKPA PGPTYGIPPR
TPTQQQQQQQ QPKPYQYKPK ESMMHTFRAP AYNPDTRKNP NSPVAHQPNV TYDYRAAGSP
YGQSTYHSSY HSSRPSQGGY IPYAPPQSYS TNAKSPTTSK PAPLTGMHQY AQSAPSSALQ
PNPYQLPPLP YSQSQGPVPR PVYSPPAGRP GSQSQPYHGG APASHTMSNP TGTSKPPMYA
TMHSSLSAQP PSSQAEYLAY VTKYPYLKNA FLRRAKTYIS PYSPNGGFTP EWAPKVSSAS
SGPLNMMPPM RPGQPSPGLG LNFGGAMSPS LPMPRPTAQF QSPDAFRQDL NKAPRPLSGA
PKWETMLKHL GTTTGQPAPS NSTTSHSPLP ALAPAPVSRP VPGGTPLAPT PMAPQTPSTS
QQPTKSASPL AIDPALQSHT LPLPPPSAVS HPTPTPLGEK PNTPQRPDYS PISDNGETRP
VPLGAAPSNV MPPAHTGETW RYS
//
