ID A0A0D0AWF7_9AGAM Unreviewed; 1012 AA.
AC A0A0D0AWF7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-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=CY34DRAFT_811438 {ECO:0000313|EMBL:KIK36218.1};
OS Suillus luteus UH-Slu-Lm8-n1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK36218.1, ECO:0000313|Proteomes:UP000054485};
RN [1] {ECO:0000313|EMBL:KIK36218.1, ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK36218.1,
RC ECO:0000313|Proteomes:UP000054485};
RG DOE Joint Genome Institute;
RA Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
RA Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
RA LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
RA Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-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}.
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DR EMBL; KN835548; KIK36218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0AWF7; -.
DR STRING; 930992.A0A0D0AWF7; -.
DR HOGENOM; CLU_001442_1_0_1; -.
DR InParanoid; A0A0D0AWF7; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000054485; 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; PF13771; zf-HC5HC2H; 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:UP000054485};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 59..100
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 346..512
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 596..742
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 112116 MW; E22A384A3B3A6C2D CRC64;
MEATPPVDVN SRSRSPTPAP LVQPDHFFGS EGAHLPPSPN SDGRTWLDPD DDPLAHRGIP
VFKPSMQEFQ DFEGYMNKIE RWGLRSGIVK VIPPKEWVDA LPGTKNQLGD VKIRTPIEQH
MLGRGGLFRQ ENVEKRKVMS VREWAELCEK EEFCAPGVED VGLHGRNVAV KTRSKRTKTR
AASTKVESIE PEDSLAQVQE EEGDVSNERP DGISAPLSPP TSVGHPQTPV STTADDLVHH
PDPSCSDQLR GDVEMTAHDD NDASEKKPAA KKRGAQSREV REAERAAKDA TFLKNFEPHK
DWLPPCTTAD DYTVEFCQKL ERQFWRNCGL GKPPWYGADT QGSVFTDETT AWNVGHLPSF
LSRLLPSSSK GLPGVNTPYL YFGMWRATFA WHVEDMDLFS INYIHFGAPK FWYAMPQGRA
AALESTMKGY FPKDISQCPQ FLRHKSFLAS PTLLAQSSCR PNFLVQRAQE FVITYPRGYH
AGFNLGFNCA ESVNFALESW IELGRRAKAC QCISDSVRID VDQLLYDRET ERLNPPAPEP
EKRQPSSKRK ALEGPESQSK RKRPKATESS TSTPVAGPSA SRVTLKLGPR PVEDVFPCCL
CTSTSRDGLF PVQDPPVGRR ELPESLSSLA TEAWMAHEEC AKVVPETWVD EVETEMSMEK
RVFGVDAIVR DRWNLKCAAC TKARQKAHGA PIQCTKGKCA KSFHVSCARD GGSSGIVFSI
LREVEKEVIL VYPNPLPLAH HTAPTSDGTT TFLDPALSQS QMQPDAVLPP PVEVEPQVLK
SIKKYDVHVL CLQHNPAIAA AKRATKQDRI KSELVGLPPM SRIKIRVSSG VFEVSLVRII
EETGSVEVLW DRGIKREFKW GSVIFGQTEG QTVVQKPSEP APELPHPSMQ VTTYPSISAA
AASLSSAIPT QVTSSTTHYA PYYAPQSHQQ YYSTNAYGSG SWSYHARYEI PTHQPMPQIP
HGYAAYYSHP AYGQPVSNSN TGHPGQAPNG AQLQWRQPYI GGMHAIVDTS GQ
//
