ID R7S562_PUNST Unreviewed; 1118 AA.
AC R7S562;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=PUNSTDRAFT_108236 {ECO:0000313|EMBL:EIN04471.1};
OS Punctularia strigosozonata (strain HHB-11173) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Corticiales; Punctulariaceae; Punctularia.
OX NCBI_TaxID=741275 {ECO:0000313|EMBL:EIN04471.1, ECO:0000313|Proteomes:UP000054196};
RN [1] {ECO:0000313|Proteomes:UP000054196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-11173 SS5 {ECO:0000313|Proteomes:UP000054196};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH687554; EIN04471.1; -; Genomic_DNA.
DR RefSeq; XP_007388266.1; XM_007388204.1.
DR AlphaFoldDB; R7S562; -.
DR GeneID; 18876153; -.
DR KEGG; psq:PUNSTDRAFT_108236; -.
DR eggNOG; KOG0958; Eukaryota.
DR HOGENOM; CLU_001442_1_0_1; -.
DR OMA; WNLKCTA; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000054196; 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:UP000054196};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 60..101
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 326..492
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 587..728
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 122166 MW; DCCCA74EC0D9CC83 CRC64;
MESVLSSRTP SLTPSRSPTP MQPVQPDHFY GSDIQLPLSP QSNGKTWLDP ADDPLAQRGI
PVFKPTMAEF RDFEGYMKAI ECWGMRSGIV KVIPPQEWRD SLPPVEPQLA NVEIKNPIEQ
NMLGGGGLFR QTNVGRRKMM TVKEWFEYCS KDEYRAPGVE EIGPYSAHRT TRTSGRTTRR
GRTAKAEPQE PVVKDEPMDD SASALLSPPR STRNLSTPAV ADEEVAILDN PPPEFSPPSA
ETKKKARARR AAKNKEAKDA EHAAKMAANA EFVKSFSAHK DWLPPKTSPE SYTPEFCREL
ERHYWRNLGL GKPAWYGADT AGSLFTDQTT SWNVAHLPSL LTRLLPASSK GLPGVNTPYL
YFGMWRATFA WHVEDMDLFS INYIHFGAGK HWYAIPQGRA SALEQTMKGF FPKDISQCPQ
FLRHKSYLAS PKTLAGALCK PNTLVQHAGE FVITYPRGYH AGFNLGFNCA ESVNFALDSW
VDLARKAQVC KCVGDSVSIN IDELLREREE ERIEAAFIRH DQKNSKENVR PRVSGSAPRK
RKPDGEGGPP KKKKKVTVKD EQLEVAAVPK PKITVKLKLG PKPEEDSFPC CLCVSSSTSD
LLRVHDLPLH AKDARSNHPW MAHEHCASVV PETWVDEIEV GEPREDGTRA TERVVFGVDG
IVKDRWNLKC SACTKPRAKA HGAPIQCTKG KCSKAFHVSC ARHGSAQGII FSVLREVEKE
VVLLGETVMD APPTELVSAP STEGASETHS STVPSEPASS PRVLKVIKKT EVQVLCSQHN
PARLEAKKSA KQDKMKNHLL ALDPMTRIKI RVSAGVFEVS LIRVISETGS VEVLWDKGVK
REFKWSSVIL GNTPEGVPVG QMPKDPAPEN LFTPRHATLA PAPSISLTEP IMPTAAQWDA
LFSYQRQKNL ALWPTTSLQQ GTQMIWPSQA QLQAAMAALS KMEQSPPSGA PSSPAVTTQP
EHFRPPTQIP PLPPTQVPSG LPSAFPIGVP GQPYVGYPAT AYQALTGTNG DCQSYGPPAA
GAVVPRSQYP NGQITWQQPY AGPPQKHGFR TGCTTPAPLD PPSRASSTIP GSMATGASSY
PSLTPSASGA VMPSTGTLSY SQLASMAAVT SNSPHNQP
//
