ID A0A4Z1IH74_9HELO Unreviewed; 1468 AA.
AC A0A4Z1IH74;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 02-APR-2025, entry version 18.
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=BCON_0082g00160 {ECO:0000313|EMBL:TGO56103.1};
OS Botryotinia convoluta.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botryotinia.
OX NCBI_TaxID=54673 {ECO:0000313|EMBL:TGO56103.1, ECO:0000313|Proteomes:UP000297527};
RN [1] {ECO:0000313|EMBL:TGO56103.1, ECO:0000313|Proteomes:UP000297527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL11595 {ECO:0000313|EMBL:TGO56103.1,
RC ECO:0000313|Proteomes:UP000297527};
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:TGO56103.1}.
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DR EMBL; PQXN01000082; TGO56103.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000297527; 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:UP000297527};
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 571..694
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..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..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..1414
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..523
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..549
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 1040..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..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..1206
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1240
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1285
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1354
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1468 AA; 164101 MW; F626DF2525EDE7F1 CRC64;
MSTATDQVVV PSEGEQSAIP QGLASPPESN NTIRTDPSSD SELSDLEFTA DEPIEPEHWE
DDGRVPVFMP TMAQFKDFNL FMDKVNKYGM KSGIVKVIPP PEWKAALPPL DDAIKTIRVK
DPIKQDIMGQ SGTYRQANIL HQRSYNLPQW RQLCDQSEHQ PPAKRGERRA NVEKVKATTR
AKASTPGGKR KPGRPSRLKT NATVDSEGGT PDRLPTPISP KTEGDSSSVK QEVNEDDTPV
KPKGGRQPKA ISVSSRRKNN RRGEAGVVDE AAFENFKYEL EGEDYSAERC EELERHYWRT
LTYAPPLYGA DMMGSLFDDK TTEWNLGKLP NILDHLGGQI PGVNTAYLYL GMWKATFAWH
LEDVDLYSIN YLHFGAPKQW YSISQGDARR FEAAMKNIWP ADAKACNEFL RHKTFLISPQ
HLLSNYNIKV NKIVHRPGEF VITFPYGYHS GYNLGYNCAE AVNFGLPSWL EYGKVAKKCD
CDQAQDSVWI NVRDLERKMN GEETEYETDF DEDEEEEDDE NETTDLPTPP DSSGDAKVKT
KTQRKRKRVK NESDEQQNVK RIRMRIKAPV NEPCVLCPND IPSEPLLPTE DGKQAHRMCA
QYIPETIVEE ADKKEVVTGI KEISKARFDL KCNYCRSKKG ACFQCSKKKC TRAYHATCAA
AAGVFVEQGE IPVFGEDGTE YKEWGIEFSC RFHRIKRDKR LDSDSLEEDD RIRNGAKELK
VGEVCQMQFY KGDIFAGTII ENRKDEETVL VDILPRGDRV EVEYKWILIP DASFFTLAKP
SEKAIPMPKS RIEAASLNTT KRQVDDIPRA EDPFVKGFTW AEFNTENIAR NAAQVKLDLS
KENQVWYYLG KNSTEARAQF TEDLKIQRHN PKGHFLDTIP KPATAAPRTS YAASYPTSTN
KISATTTKMP TANPSNMGPA VQAMQKMAAT KLVNQPAPSS GTSAPFVARS EKPYVYKPRK
SEDGYHSGLI DAQSYHSQQA FLRQSAASRP VQVPAVGLNF GTDPRFQNKP ASPAPTSTTP
PATTSTNQSA VVPPRAAYTP KNSYAPQVSY PSQVNYAPQV KYAPPRQPHQ ATTPRQSQPT
ASPLAPPNTN YRPTQSLAKG NNPFSNRAAA PKMGNVFAKY LYLQIEHNRS PMEYKSPYRE
GGGFMNGYQG NWTEHLKKTL FAKSGSSTAS PPTSISSYTG GVGRKASYPT SYTPQSSRGS
YSSNGSQIYS PATSSARPSY ASPSIPRHQQ TPTQQVTPKP YDTNQWERKD SPLHPAIRKE
YSSMFHNHHV PQPQGQQENP QQQGHQQHHK SHGSTQYQNS SYLPSGGQGS PTQSRFASQA
PKATESKQAQ QIEQSQKSQQ LQPPQSQPTP QVAQKTGHNP LSQPQPVVKA TLITPPSYSP
PFTQREPTQQ PINASNHSQV SPQPPQQEAK PIYPHQQYFQ NLNASHVQPQ TFAPPPQTHD
LPDVPIDSES LIEDMLKNLR KVTTNTTK
//
