ID A0A444SB20_VERDA Unreviewed; 1610 AA.
AC A0A444SB20;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-OCT-2025, 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=VDGE_07479 {ECO:0000313|EMBL:RXG50560.1};
OS Verticillium dahliae (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=27337 {ECO:0000313|EMBL:RXG50560.1, ECO:0000313|Proteomes:UP000288725};
RN [1] {ECO:0000313|EMBL:RXG50560.1, ECO:0000313|Proteomes:UP000288725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Getta Getta {ECO:0000313|EMBL:RXG50560.1,
RC ECO:0000313|Proteomes:UP000288725};
RA Gardiner D.M.;
RT "Genome of Verticillium dahliae isolate Getta Getta.";
RL Submitted (DEC-2018) 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:RXG50560.1}.
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DR EMBL; RSDZ01000005; RXG50560.1; -; Genomic_DNA.
DR Proteomes; UP000288725; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 115..156
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 399..562
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 650..773
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..95
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..255
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..311
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..607
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..628
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..991
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1086
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1159
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1184
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1230
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1403
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1503..1512
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1610 AA; 177260 MW; 3F260A4FA4BB4CD2 CRC64;
MSTEAPSALA SAPTQVSLAP EAAQTQTGCT NDVGNTDGHT QDRVANAEHD APADHIECAK
PTFLHSPPDS NNAAKSDGSD SELSELDDDA VDPADEPPKE DDIGQVEPDH YSGTVPVFRP
TMHQFKDFKR FMEKIDHYGM QSGIVKIIPP EEWKNSLPEL DELVKQVRVR EPIKQDIMGS
GGTFRQVNIL HQRSYNVPQW RKLCEQSEHQ PPARRGERRA NADKPRPATR TRAAASSAPK
PRAAPAKKRG GKRGAKNSGK QKKDADDAET EDRPMTPVSP REDADEGKIK TEAVVDSVET
EDAEEEEEEE AAPTVGRMGR MGGVRPSKGA TQSVSARRKY SKREGSAKID EEAFKDFDYR
MDVSDYTPER CEELERAYWK TLTYAPPLYG ADLMGTLFDE STDTWNLNKL PNLLDVLGSK
VPGVNTAYLY LGMWKATFAW HLEDVDLYSI NYLHFGAPKQ WYSISQADAK RFEAAMKNIW
PTDAKACDQF LRHKGYLISP QQLKQNYNIT VNKCVSYPGE FVVTYPYGYH SGYNLGYNCA
EAVNFALDSW LPMGKIAKRC QCPQAQDSVW IDVYDIERKL RGEELEYEEY TDDDGDEEED
EDMEEPESTN APGSRAVKIK APSRKRKRDA KDKDEKKVKK IRLRIKARAE PPCCLCPNDI
ASAELIPTND GRKAHRMCAH YLPETYIETI DDKEVVCNVA NVAKDRLDLK CLFCRSKRGA
CFQCSQKKCA RAYHATCAAA AGVFVEEAEV SVWGEDGTEY KEQAFEFSCR FHRTKRDKKV
DGDSLDDDER ILNAAKAVKE GEICQLQYFK GDIFAGVVVE NRKDERMLLV DILPNGARVE
VEWKWLLVAD PSDYHLPKAS AKAIPMPTSQ KAKQELNAKR AVDEVPRKDD TFVDGGFTWA
EYHTCEPIHN KGQAKVDLDK DMQLWYYLGK TSTEAKAQYT ESPTLQRHNP RSNYLDTLPK
PAKPPKPVSV TQRRPSQVPQ RPSIPGPPRP SPLSTSSVPA PVQGPAQGPM PMPSLPNAVN
VEKPYVYKPR KPIDGAWFKT QQFTNQQFAL KMSNSPSPAP NGQQPGYGVD SRIAGQQYPQ
PSQYSQHRFI PSYAPAYNPQ TATYGAQGNA PPNYGQPQQQ QQQQRTWSTP SSMNQPSPYQ
SGQYNSQQRS QQGQQGTSYT DSNRPLQVHQ YQPVVQQSST PSQPAHVSPA QYAATQQIAT
NSQKQSQQQS QPYNAAQQQV QVQHLQQSPA SFTADQAQTG PDRYHTPYNA TQDNTILARA
CIKQWFTLEP DESDYRKRCS PPGKPYFDGD TLSDASAGTE LNVSAGGGAA SRNRLRFVND
TGADANQQDA LNLAPQPPSN QESASEIKPS KPQAPKVQYK IPEKVTPVPL PAMYRAARSK
TGPAPTPTPG PTKAAPQAQP QTPEVARAPT STLPSPTSNG ALGSTSSAQS PNAQSKTARI
SETPVPLPHQ KAANSTPRTK ASGAMFGHAS TASPTKTVVS TPDSTPAQPL VPAQTSTSPD
SIAAAAQQAS AAYTQNVTPS RPPSQPTQVS DRAAVETPVP LPRLPVKVTP VPLPPQALQV
LSAGNPVSKP SGYTGEAISE TPILPPVRAP MATTQTSAEV DDMDRGRGVH
//
