ID A0A2X0LAK7_9BASI Unreviewed; 1454 AA.
AC A0A2X0LAK7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, 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=BZ3500_MVSOF-1268-A1-R1_CHR8-2G10281
GN {ECO:0000313|EMBL:SCZ96542.1};
OS Microbotryum saponariae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=289078 {ECO:0000313|EMBL:SCZ96542.1, ECO:0000313|Proteomes:UP000249723};
RN [1] {ECO:0000313|Proteomes:UP000249723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; 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:ARBA00000040};
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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; FMWP01000088; SCZ96542.1; -; Genomic_DNA.
DR STRING; 289078.A0A2X0LAK7; -.
DR Proteomes; UP000249723; Unassembled WGS sequence.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 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; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 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 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:UP000249723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 280..324
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 609..774
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 935..1052
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1454 AA; 157003 MW; 3F281A38A2C8128B CRC64;
MGQDDQPRSV VPPPPARTMQ AGQVVVERAA PVEAGVLVVS ACARPLTVSR SEPISLISRS
AVATTAPTAA FPDDTPFPEG VVQGSTMQGI ESSDVSPEST RTPVVPATTN TPVAVPASAP
VSACAAPPAA AAAAASAPAP PPPLPRDDQV HDERLPPPPP LVNQPQQPKP KKPRGRKKKE
LDRDQAPPTP AASTASSSES IFTAIPSFIS SLDLSDSEPD SSASEDEFGQ PKPPKQPAYD
SQGRARPRPS YYYDADYDPA HHSALEPIKK RGRRGGLKGV PVFEPTIEDF ERNGGFYGYV
KRIEKYGRRS GIAKVIPPKE WSDALPSTTD KLRDIRLREP IEQIMMGQQG VYRVTNVAKT
RIWNPAQWKQ MADSSKFAPP DFKKEAEKGD RTDRKPVLGG SNASASTSTS ATPNKKGSRK
AAGGEGEADA DDEAELEAVG KRKAAPQTPA NGKGKEPETP SQTRSGTRFG SDRKNENGRP
TTATPSESPT TRKASIPIAT EDSTTSTAAP TPISVGAPHA TKDSATSSAS LASATKPARV
KRASNLQRAE PTEAEWSAFV ENYAELPHGM KKSDYTVELM RDIERRYWRT LTFGEPAMYG
ADMKGSIFSD ETQAWNVAHL GDLLPKLAPK SCQIPGVVSP YLYFGMWRAT FAWHVEDADL
YSINYIHFGA PKFWYSVPQE QSERFERVME GYFQQDRTKC SQFLRHKSFL ASPRVLAGSN
ITLNRCMQLP GEFILTYPKG YHSGFNLGFN CAESINFATE RWLPLGKVSK SCFCIGDSVN
IDVDVWLTDA ARKEAEARGE VWPPRKAMPT PPPEDDLEAA AAKMASFAGP GQGLAISTIS
STSSHPHGPA VFEVPKLEAA PSSSGRKRMF SAKAAELELG QAQVAAASTT ISPNSQPHIH
PTSTNGNVSH PPLKKRAKLS SPVASTLNES AMPLPYPCAL CPERSTEGLI RIGEPAQFKM
LAHRVCVMFT PATWIETVPE TGEEVVRGFL DIEKARWKLK CQLCEEKHGT KVQCTKGKCP
KAMHVTCGLR LDSGAFLDAT VGGLSMLDLN RVEGASPKPK LMDNKPLEPV VMTDASAMVV
DDVQPAAAAP VDAAITSTSE NAPASTFNSA PMPAPALAPP AIIEESNDIR LTILCRQHNP
AWQKLEVERK YEDLKARVAA LPENSRLQVK TNNGVFDVTY LTNLPHKSSI GILFDDGKRH
EVRWRAILWP ESPEAIKRKA EIAAKIAEDK AAYDRPPTKK RISSPDDGNM HHHSYSGRGS
PYAHTSLAAA YMHQQPAPGY FYAPQMGDYA GPGPQQQMML PNMGNAPPYG WRGHYYGGDP
VASPASYPYP PLMHPAQAQG WSGPPPPPLG EYAGPYGHQH QQARNPSQCA YEHPSASPPS
SGYKPAPLGS SIESQHAHRN SYPPSASSPI STFVVPRPQD AHLAVPNPAP PNSSRHSLKN
LLSPVVDDVA VLGH
//
