ID A0A8H6AVG8_9HELO Unreviewed; 1461 AA.
AC A0A8H6AVG8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 14.
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=Bfra_004475 {ECO:0000313|EMBL:KAF5874466.1};
OS Botrytis fragariae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1964551 {ECO:0000313|EMBL:KAF5874466.1, ECO:0000313|Proteomes:UP000531561};
RN [1] {ECO:0000313|EMBL:KAF5874466.1, ECO:0000313|Proteomes:UP000531561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BVB16 {ECO:0000313|EMBL:KAF5874466.1,
RC ECO:0000313|Proteomes:UP000531561};
RX PubMed=32648525;
RA Wu Y., Saski C.A., Schnabel G., Xiao S., Hu M.;
RT "A high-quality genome resource of Botrytis fragariae, a new and rapidly
RT spreading fungal pathogen causing strawberry gray mold in the U.S.A.";
RL Phytopathology 0:0-0(2020).
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:KAF5874466.1}.
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; JABFCT010000007; KAF5874466.1; -; Genomic_DNA.
DR RefSeq; XP_037193412.1; XM_037334878.1.
DR GeneID; 59258570; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000531561; 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:UP000531561};
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..45
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..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..36
FT /note="Polar 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 1009..1031
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1169
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1232
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1278
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1347
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1461 AA; 162879 MW; 68AFA538E2A2BCAD CRC64;
MSTATDQVVV PTDGEQSATP QGLASPPESN NTIRTDPSSD SELSDLEFTA DEPIEPEHWE
DDGRVPVFMP TMAQFKDFNL FMDKVNKYGM KSGIVKVIPP PEWKAALPPL DDAIKTIRVK
DPIKQDIMGQ SGTYRQANIL HQRSYNLPQW RQLCDQSEHQ PPAKRGERRA NVEKVKATTR
AKASTPGGKR KPGRPSRLKT NATVDSEAGT PDRLPTPISP KTEGDSSSVK QEVNEDDTPV
KPKGGRQPKA ISVSSRRKNN RRGEAGVVDE AAFENFKYEL VGEDYSAERC EELERHYWRT
LTYAPPLYGA DMMGSLFDDK TSEWNLGKLP NILDHLGGQI PGVNTAYLYL GMWKATFAWH
LEDVDLYSIN YLHFGAPKQW YSISQGDARR FEAAMKNIWP ADAKACSEFL RHKTFLISPQ
HLLSNYNIKV NKIVHRPGEF VITFPYGYHS GYNLGYNCAE AVNFGLPSWL EYGKVAKKCD
CDQAQDSVWI NVRDLERKMN GEETEYETDF DEDEEEEEED ENETTDLPTP PDSSGDAKVK
TKTQRKRKRV KSESDEQQNV KRIRMRIKAP VNEPCVLCPN DIPSEPLLPT EDGKQAHRMC
AQYIPETIVE EADKKEVVTG IKEISKARFD LKCNYCRSKK GACFQCSKKK CTRAYHATCA
AAAGVFVEQG EIPVFGEDGT EYKEWGIEFS CRFHRIKRDK RLDSDSLEED DRIRNGAKEL
EVGEVCQMQF HKGDIFAGTI IENRKDEETV LVDILPRGDR VEVEYKWILI PDASFFTLAK
PSEKAIPMPK SRIEAASLNT TKRQVDDIPR AEDPFVKGFT WAEFNTESIA RNAAQVKLDL
SKENQVWYYL GKNSTEARAQ FTEDLKIQRH NPKGHFLDTI PKQATAAPRT SYAASYPTST
NKISATTTKM PTANTSNMGP AVQAMQKMAA TKLVNQPAPS SGTSAPFVAR SEKPYVYKPR
KSEDGYHSGL IDAQSYQSQQ AFLRQSAASR PVQVPAVGLN FGTDPRFQNN PASPAPTSTT
PPATASTNQS AVVPPRAAYT PNNSYAPQVS YPPQVNYAPQ VKYAPPRQPQ PTASPLAPPN
TNYRPTQSLA KGNNPFSSRA AAPKMGNVFA KYLYLQIEHN RSPMEYKSPY REGGGFMNGY
QGNWTEHLKK TLFAKSGSSS ASPSTSISSY TGGVGRKASY PTSYTPQSSR GSYSSNGSQI
YSPATSSARP SYSSPSIPRH QQTPTQQVTP KPYDTNQWER KDSPLHPAIR KEYSSMFHNH
HVPQPQGQQQ NPPQQGHQQH NHKSHGSTQY QDSSYLPSGG QGSPTHSGFA SQAPKIIESK
QAQQIEEPQK SQQLQPPQSQ PTPQVAQETG HNPLSQPQPV VKATLNTPPS NSPPLTQSEP
SQQPINASNQ SQIPAQPPQQ EAKPIYPHQQ YFQNLNASQV QPQTFAPPPK THDLPDVPID
SESLIEDMLK NLRKVTTSTT K
//
