ID A0A4Z1J9V9_9HELO Unreviewed; 1469 AA.
AC A0A4Z1J9V9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 02-APR-2025, entry version 19.
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=BOTNAR_0001g00820 {ECO:0000313|EMBL:TGO70406.1};
OS Botryotinia narcissicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botryotinia.
OX NCBI_TaxID=278944 {ECO:0000313|EMBL:TGO70406.1, ECO:0000313|Proteomes:UP000297452};
RN [1] {ECO:0000313|EMBL:TGO70406.1, ECO:0000313|Proteomes:UP000297452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL2120 {ECO:0000313|EMBL:TGO70406.1,
RC ECO:0000313|Proteomes:UP000297452};
RA Valero-Jimenez C.A., Tapia P., Veloso J., Silva-Moreno E., Staats M.,
RA Valdes J.H., Van Kan J.A.L.;
RT "Comparative genomics of Botrytis spp.";
RL Submitted (DEC-2017) 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:TGO70406.1}.
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DR EMBL; PQXJ01000001; TGO70406.1; -; Genomic_DNA.
DR STRING; 278944.A0A4Z1J9V9; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000297452; 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:UP000297452};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 65..106
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 318..481
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 572..695
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..197
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..550
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1026
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1083
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1177
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1240
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1286
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1352
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1469 AA; 163923 MW; 112BAB7C98906D95 CRC64;
MSTATDQVVV PSEGEQSAIP QGLASPPESN NTIRTDPSSD SELSDLEFTA DEPIEPEHWE
DDGRVPVFMP TMAQFKDFNL FMDKVNKYGM KSGIVKVIPP PEWKAALPPL DDAIKTIRVK
DPIKQDIMGQ SGTYRQANIL HQRSYNLPQW RQLCDQSEHQ PPAKRGERRA NVEKVKATTR
AKAPTPGGKR KPGRPSRLKT NATVDSEGGT PDRLPTPISP KTEGDSSSVK QEVNEDGTPV
KPRGGRQPKA ISVSSRRKNN RRGEAGVVDE AAFENFKYEL EGEDYSAERC EELERHYWRT
LTYAPPLYGA DMMGSLFDDR TTEWNLGKLP NILDHLGGQI PGVNTAYLYL GMWKATFAWH
LEDVDLYSIN YLHFGAPKQW YSISQGDARR FEAAMKNIWP ADAKACSEFL RHKTFLISPQ
HLLSNYNIKV NKIVHRPGEF VITFPYGYHS GYNLGYNCAE AVNFGLPSWL EYGKVAKKCD
CDQAQDSVWI NVRDLERKMN GEETEYETDF DEDEEEEEED ENETTDLLTP PDSSGDAKVK
TKTRRKRKRV KSESDEQQNV KRIRMRIKAP VNEPCVLCPN DIPSEPLLPT EDGKQAHRMC
AQYIPETIVE EADKKEVVTG IKEISKARFD LKCNYCRSKK GACFQCSKKK CTRAYHATCA
AAAGVFVEQG EIPVFGEDGT EYKEWGIEFS CRFHRIKRDK RLDSDSLEED DRIRNGAKEL
KAGEVCQMQF YKGDIFAGTI IENRKDEEIV LVDILPRGDR VEVEYKWILI PDASFFTLAK
PSEKAIPMPK SRIEAASLNT TKRQVDDIPR AEDPFIKGFT WAEFNTESIA RNAAQVKLDL
SKENQVWYYL GKNSTEARAQ FTEDLKIQRH NPKGHFLDTI PKPATAAPRT SYAASYPTTN
KTSATATKMP IANTSNVGPA AQVMQKMAAT KLANQAAPSS GTSAPFVARS EKPYVYKPRK
SEDGYHSGLI DAQSYQSQQA FLRQSAASRP VQVPAIGLNF GTDPRFQNNP APPAPTSTTP
PAIASTNQSA VVPPRAAYTP NNSYAPQVSY PPQVNYAPQV KYAPPRQPHQ AATPRQSQPA
ASPLAPPNTN YRPTQSLAKG NNPFSSRAAA PKMGNVFAKY LYLQIEHNRS PMEYKSPYRE
GGGFMNGYQG NWTEHLKKTL FAKSGSSTAS PPTSISSYTG GVGRKASYPT SYTPQSSRGS
YSSNGSQIYS PATSSARPSY SSPSIPKHQQ TPTQQVTPKP YDTNQWERKD SPLHPAIRKE
YSSMFHNHHV PQPQDQQQNP QQQGHQQHNH KSHDSIQYQN SSYLPSGGQG SPTQPGFASQ
APKTTEFKQA QQTEEPKKSQ QLQPPQSQPT PQVAQTIGHN SSSQPQPVAK ATLITPPSYS
PSLNRTEPSQ QPINASNQSR VPPQSPQQEA NPVYPHQQYF QNLNSSRVQP QTFAPPPQTH
DLPDVPIDSE SLIEDMLKNL RKVTTGTAK
//
