ID A0A316YK66_9BASI Unreviewed; 631 AA.
AC A0A316YK66;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, 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};
DE Flags: Fragment;
GN ORFNames=FA10DRAFT_242964 {ECO:0000313|EMBL:PWN89466.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN89466.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN89466.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN89466.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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}.
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DR EMBL; KZ819637; PWN89466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316YK66; -.
DR STRING; 215250.A0A316YK66; -.
DR InParanoid; A0A316YK66; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000245768; 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; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000245768};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..35
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 224..399
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 440..587
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 92..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 408..436
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 93..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 631
FT /evidence="ECO:0000313|EMBL:PWN89466.1"
SQ SEQUENCE 631 AA; 71922 MW; 09C37A89D49F4F7F CRC64;
MDDFRDFYSF CERIDHWGMR SGIVKVVPPA EWTGKLPKLD EGEVKRLRAV RIKNSISQMF
SKAGGGAFHQ KNIVHPAKVV NAKQWADLCA SKEQRGPDME RMKGNARAEA KARKQELRMG
HFAVPTDDND DDDDDGEQKE EDGVRTRSGG TPSRETAKHG QKAEGKVKMA DRTTEAEWNA
FDYENGWCHE AGPKATADDW KDEEVCRAIE KEYWSGLIWG KPPMYGADLE GTLFTDETKD
WNVGHLDNVL TRLKLKHRLK GVTTPYLYFG MWRATFAWHV EDVDLYSINY IHFGAPKQWY
SIRQSDRQRF ELAMAGAFPG DSSRCRHFMR HKSYLASPSF LASNNIKPLR LVQHAGEFVI
TYPYGYHSGY NLGFNCAESL NFALESWIPI GRRAGHCLCD PDAVHMDIDA LLEESAELEE
MERRREERQR GQVEHEARLE DNCVFCPYNL DDDLVPLRAD AKARYAHRFC TNFMPECWVG
EDDDDDRGPG EVVMGFDSIN KARWSLKCQL CATPQLAKKG AKVQCTYSKC SRTTHAACAL
KDTSGWLLDV VGDRAADRLE GKTTGTDEIE EDDEEPTRMV VLCKQHNPEQ KQREAVRKAL
VLKACVTRLK EGQNVRVRTS RGVWMTVLVE V
//
