ID A0A4Z1KNJ3_9HELO Unreviewed; 1469 AA.
AC A0A4Z1KNJ3;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 02-APR-2025, entry version 17.
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=BPOR_0265g00070 {ECO:0000313|EMBL:TGO86936.1};
OS Botrytis porri.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=87229 {ECO:0000313|EMBL:TGO86936.1, ECO:0000313|Proteomes:UP000297280};
RN [1] {ECO:0000313|EMBL:TGO86936.1, ECO:0000313|Proteomes:UP000297280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL3349 {ECO:0000313|EMBL:TGO86936.1,
RC ECO:0000313|Proteomes:UP000297280};
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:TGO86936.1}.
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DR EMBL; PQXO01000264; TGO86936.1; -; Genomic_DNA.
DR STRING; 87229.A0A4Z1KNJ3; -.
DR Proteomes; UP000297280; 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:UP000297280};
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 996..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1413
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 1010..1026
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..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 1186..1226
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1286
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1356
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1469 AA; 164253 MW; C694B474C0AD17BC CRC64;
MSTATDQVVV PSEGEHSTIP QGLASPPESN NTIRTDPSSD SELSDLEFTA DEPVEPEHWE
DDGRVPVFMP TMAQFKDFNL FMDKVNKYGM KSGIVKVIPP PEWKAALPPL DDAIKTIRVK
DPIKQDIMGQ SGTYRQANIL HQRSYNLPQW RQLCDQSEHQ PPAKRGERRA NVEKVKATTR
AKGSTTGGKR KPGRPSRLKT NATVDSEDGT PDRLPTPISP KTEGDSSSVK QEVNEDDTPV
KSRGGRQPKA 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 PDSSGDAKIK
TKTQRKRKRV KSESDEQQNV KRIRMRIKAP VIEPCVLCPN DIPSEPLLPT EDGKQAHRMC
AQYIPETIVE EADKKEVVTG IKEISKARFD LKCNYCRSKK GACFQCSKKK CTRAYHATCA
AAAGVFVEQG EIPVFGEDGT EYKEWGIEFS CRFHRIKRDK RLDSESLEED DRIRNGAKEL
KLGEVCQMQF YKGDIFAGTI IENRRDEETV LVDILPRGDR VEVEYKWILI PDASFFTLAK
PSEKAIPLPK SRIEAASLNT TKRQLDDIPR AEDPFVKGFT WAEFNTESIA RNAAQVKLDL
SKENQVWYYL GKNSTEARAQ FTEDLKIQRH NPKGHFLDTI PKPATAVPRT SYAASYPTST
NKFSATTTKM PIANTSNIGP GIQALQKMAA TKLVNQPAPS GTSAPFVARS EKPYVYKPRK
SEDGYHSGLI DAQSYQSQQA FLRQSAASRP VQVPAVGLNF GTDPRFQNNS ASPAPSSTTP
PATTSTNQSA VVPPRAAYTP NNSYAPQVSY PPQVNYAPQV KYAPPRQPHQ AATPRQSQTT
ASPLAPPNTN YRPTQSLAKG NNPLSNRAAA PKMGNVFAKY LYLQIEHNRS PMEYKSPYRE
GGGFMNGYQG NWTEHLKKTL FAKSGSSTAS PPTSISSYTG GVGRKTSYST SYTPQSSRGS
YSSNGSQINS PAASSARPSY ASPSIPRHQQ TPTQQVTLKL YDTNQWERKD SPLHPAIRKE
YSSMFHNHHV PQPQDQQQTS QQQGHQQHSH KTHSSTQYQN SSYLPPGSQG SPAQYGFASQ
APKTAESEQA QQLQEPQKSQ QLQPPQPQIT PQAAQETGQN PLSQPQPVVK ATLVTPPPYS
PPLAQREPSQ QPINVSHQSQ VPPQPPQQEA KPIYPHQQYF QNLNASQVQP QSFAPPPQTH
DLPDVPIDSE SLIEDMLKNL RKVTTSTTK
//
