ID A0A0M8N828_9HYPO Unreviewed; 1125 AA.
AC A0A0M8N828;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=ESCO_001799 {ECO:0000313|EMBL:KOS21930.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS21930.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS21930.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) 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 -!- 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:KOS21930.1}.
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DR EMBL; LGSR01000006; KOS21930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8N828; -.
DR STRING; 150374.A0A0M8N828; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000053831; 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; IPR001965; Znf_PHD.
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 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:UP000053831};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 160..201
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 429..592
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 683..806
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..638
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..668
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1125 AA; 123814 MW; CFE4165D41A824C3 CRC64;
MSTVAASATG GPPEALPLDP DAQHHATDDK IDSCSSSSAS IADSAVKNRP RPEPAFLHSP
PDSNNADKSE ASDSELSDLD EEPVLDDAPV PPAPLPPQHQ QQQHQQSQQP ASLPEGELEN
DDDDDDDDDD DDEAAAAADG NPDVDVDIGE VLPADWSGNV PIFRPTMDQF KDFKLFMQTV
DSYGMKSGII KIIPPAEWKA AQPPLDDLIK QVRVREPIKQ DIMGSNGTYR QVNILHGRSY
NVPQWRQLCE QSEHQPPARR GERRANADKS RLQRARQAAA KSAPATANSK PRGRGRPPKT
RGKQKKEDEA RPMTPVSPKA DSQEVRDNVV PSVEKDGEDE ARETTPQPTF RRMGAVSKPK
AQSTSARRKY ARREGSAAID EAAFRDFDYR MDISDYTPDR CEELERVYWK TLTYAPPLYG
ADLMGTLFDD RTEVWNLNKL PNVLDVLGTK VPGVNTAYLY LGMWKATFAW HLEDVDLYSI
NYLHFGAPKQ WYSISQADAR RFEAAMKSLW PAEAKACNQF LRHKAFLISP QHLLQNFGIK
VNKVVSYPGE FVVTYPYGYH SGYNLGYNCA EAVNFALESW LDMGKIAKKC ECAQAQDSVW
INVYEIERKL RGEDTEFEET EDEEDEDEDE DEEDDELSGL PTPPAGHGVR VKGAGRKRKR
GPGDKSTKAK VKKIKLRLNV KVEPPCCLCP NDIPGLELLP TITGRKAHRL CALYIPETYI
DLIDDKEVVS NVAGIHKDRL ELKCLFCRSK RGACFQCSQK KCARAYHATC AAAAGVFVED
QDVPVFGEDG KEYKEQAFEF SCRFHRTKRD RKLDCAALEE EPRILEAAQA LKKGDICQMQ
FFKGEIFAGI VVENRPSEQT FLINILPNGK AKDELNAKRQ HDDKPRKDDP FVEGGFTWVE
FNTLDTKNKD QAKVDLSKPD QIWYYLGKNS TEARAQFTED PSKPRFNPKG NFLDTSPNGT
AAGICFIAFH RVRLGPFSSA SFSHELGRST HSSETGAGAS PRFPIGIANA SPMQTSRSTD
AVCVTTKSGS GNTIRQAEIL AGASTLTLAG PGTGTGTCIC ICIYICSITG TGAGTGVGAG
ASASIGTRNS LGTNFSTSTR SGTSTSTSLS TKAVQDAAAG SHGPY
//
