ID A0A6A5QT94_AMPQU Unreviewed; 1360 AA.
AC A0A6A5QT94;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, 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=BDU57DRAFT_183919 {ECO:0000313|EMBL:KAF1918010.1};
OS Ampelomyces quisqualis (Powdery mildew agent).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Ampelomyces.
OX NCBI_TaxID=50730 {ECO:0000313|EMBL:KAF1918010.1, ECO:0000313|Proteomes:UP000800096};
RN [1] {ECO:0000313|EMBL:KAF1918010.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HMLAC05119 {ECO:0000313|EMBL:KAF1918010.1};
RA Haridas S., Albert R., Binder M., Bloem J., Labutti K., Salamov A.,
RA Andreopoulos B., Baker S., Barry K., Bills G., Bluhm B., Cannon C.,
RA Castanera R., Culley D., Daum C., Ezra D., Gonzalez J., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B., Goodwin S., Spatafora J., Crous P.,
RA Grigoriev I.;
RT "101 Dothideomycetes genomes: a test case for predicting lifestyles and
RT emergence of pathogens.";
RL Stud. Mycol. 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}.
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DR EMBL; ML979134; KAF1918010.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000800096; 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 FunFam; 2.60.120.650:FF:000047; Putative jumonji family transcription factor; 1.
DR FunFam; 3.30.40.10:FF:000377; 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:UP000800096};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 68..109
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 344..507
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 600..724
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..58
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..214
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..544
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..574
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..948
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1084
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1360 AA; 152513 MW; DD909809E64DDDC6 CRC64;
MEAPSEIVPS VEAPPLQVDE ALPKAALTPP TSEDNDKRDE RMSSELSDID SDDGEDIEPD
HYFEGGKIPV FKPTMDQFRN FKRFIDKIDR HGMKSGIVKV IPPAEWRESL PDLSEAVKSI
KVKNPIMQEF AGQHGIYTQA NIEKQRSYNL PEWRSVTDEP HHQPPAKRGE RRKAAAEAPS
RTRSTRAQAA PAKTEDTSPA PRRGPGRPSR RRQVKKEPVD EDENDDDGAS VDVPPTPTSP
GGEDKKPSRR TRKDPRSDAT PTKARGRQPK TVDQKKSVSS RRLNNRGAVA DYVDEAAFEQ
FDYHLPGLDE FSVERCKELE DNYWKTINYG QPMYGADMPG SLFDDRTTSW NVAKLPNLLD
ILGTKVPGVN TAYLYLGMWK ATFAWHLEDV DLYSINYIHF GAPKQWYSIS QEDARRFEAA
MKSIWPNDAK HCSQFLRHKT YLISPQRLEK DFNIKVNRLV HYEGEFVITY PYGYHSGYNI
GYNCAESVNF ANESWLSYGR IAKKCNCESD SVWVDVNEIE RKLRGEPTPE YYEETDDEEE
EDGDDRLPTP PRSVAGKPKG KAGRKAANNK RKRGAKEPEE PPKLKRVRRI RIRIKIPGRG
MPCILCPNDV EYDELLPTDT GMKAHRLCAD YTPETYIISK AEAGDTVCNV SAIGKDRLEL
KCNYCRSKRG AVFQCSQKKC TRAFHATCAV AAGVQVDLGP MPTFDEEGTE YFYDGYDFRC
RFHRPKKRNN KTVDVEALEK DKFVLNYGKT LKPRDVIQFQ YVGGEMYQIY GAQVVENRPG
EQAVLVDVLP DGDRVEVEWK YILKLHPDES QRPKPSANAK PLPEHMKESD ASLDITNRTD
GVPEIGDPFH DPHAEHKWQE WHTAPEVTQR VAKVDFSKEN QLWYYLGRPS TEARPQYTED
PAKQRNNPKS SFLETVKPPP PPVPAFAQRS YPASYPLKPA PIAVPPRTPS QQQTHASNRP
YQYRPKESYM TSWKSPVYNP DTRKNPNSPV AHQPNVSYDH RPPSQPQGQP VYQGYHHYRP
SPPGQQQQFQ YHPYVPPQAP STPNWRTQPT TSGSMLNGTN QYAHSSQSKA QPSSPSAAHP
NSGSLPQLPP YPWSQGPGQN LSQSPYRPVG PAPSGRASIS SMLSNPTGTP KSTKYADAPS
SIVYAAKSST EYLAYLLIYP YLKNAYLRRA KTYVSPYSPG GGFTESWMPK VPNPGTPASV
APSPSAPTPP QAQFYGQQQT PSLPAPKPAA QFQSSDAFQR DMARTNQPTD GAPKWEQMLK
QLATSTGTAS MPVASAGQTQ ATHPYYAPPQ RSSMSHEMPS GMQPSQGYTP PQLPAREPQR
PTPSPISDDG KEAGGVQANL PPAPLQPAPT LHGAETWRYT
//
