ID A0A2N3N3M2_9PEZI Unreviewed; 1394 AA.
AC A0A2N3N3M2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 02-APR-2025, entry version 21.
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=jhhlp_005622 {ECO:0000313|EMBL:PKS07025.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS07025.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS07025.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS07025.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(2017).
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:PKS07025.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NLAX01000701; PKS07025.1; -; Genomic_DNA.
DR STRING; 41688.A0A2N3N3M2; -.
DR VEuPathDB; FungiDB:jhhlp_005622; -.
DR InParanoid; A0A2N3N3M2; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000233524; 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:UP000233524};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 120..161
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 411..574
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 659..782
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..267
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..613
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1110
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1271
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1394 AA; 153064 MW; 3D430499551DDC6B CRC64;
MSPEADSATA LVSVACVDST PAPQVRFDIT PQPIADKPGT TIDDADPEEL PEIRCAKLGP
VRSSPKPVAT TAVDPDDSEL SDLDDNILDV TMSDPPVPAA EEPPVDDIGE IVPDHWSGTV
PVFKPNMHQF KDFKLFMEKV DSYGMKSGII KIIPPQEWKD SQPNLDEMVK QIRVRDPIKQ
EIMGSGGAFR QVNFLHGRSY TLRQWRDLCE QSEHQPPARR GERRMNRERP KPAPRPKPAP
KEKEEKADSG TPKKRGRGRP PKKKNTNKKT APKETPLEDR PMTPVSDKEH PEGENPMETP
AKPDAPAEEG GADTAVRSIE EDEDQPTSAR RMGGMIQKSK TKTQSTSARR KYSRREGSVM
IDEEHFKDFD YRMDVSDFTA ERCEELERIY WKTLTYAPPL YGADLMGTLF DDKTEIWNLN
KLPNLLDVMG TKVPGVNTAY LYLGMWKATF AWHLEDVDLY SINYLHFGAP KQWYSISQAD
ARRFEAAMKS IWPTEAKACD QFLRHKSFLI SPTHLLNHFN IKVNKCVSYP GEFVVTYPYG
YHSGYNLGYN CAEAVNFALD SWLPMGKIAK KCECALAQDS VWVDVYDIER KLRGEETEYE
ETDEEDEESD VEDPSTLPTP PDTTSPVGRV PGRKRKRAAG EKKTPRPKKI RLRPKIKEEP
PCILCPNDIP GAEILPTETG QKAHRMCALY LPETYIETVD SVETVMNVAS ITKERKELRC
LFCRSKRGAC FQCSQNTCSR SYHPTCAAAA GVFVEEGEVP VFGEDGTEYK EQAFEFSCRF
HRTKRDRRLD GDQLEKDELI IKAAKALKPG EICQIQYFKG DIFAGVVVEN RREEETLLLD
IIPKGCVSAI VSPHYQGLTL DSDRIETEWK WLLLPDPSDY HLPKASANAL PMPSSQKAKK
KLNAKRAADE VPRKDAPFVD GYTWAEFTAY EPTNPARAKS DLSKPETLWH YLGETSTDAK
AQYTEDPSRR QHNVKSNFLD TIPKPPKPNK AAPANVATAA AGTRPYAYKQ RAPSASTTGG
GKADSPYLYG TVPKAVGSTV QFGPDPRFGS ASYQPQHVFS VQPASQPGAP NHQANGVSRP
DFSVHPQYSI SPNQNTSPYG RYGSSPSSSS LLGTQGAHPA GHDPGREAHL HLQRMAQARA
LAQQSGNSGS SPVTSIGRPY MSTFQVIPTT TGAKAGPVSS KQPKLGNAEK PTKQPVAYTV
PAKQTPVPLP AKYMAALSGS QQAPQPQPAA AAPTSTPAPQ LGASSAQTPS AQAPAPTSVT
APAPASTTAT PLAKQTATQP VRPETQPKPA ATRISTTPIP LPPLPSLSRP NEPTAAPRVE
VKGEATTITL AQLLQQPGST LPPQMPSAPE AKYGASAATA PELADVPADS SSFVEKLMFN
LHSASSQRPS EPQS
//
