ID A0A165BTX8_9APHY Unreviewed; 1194 AA.
AC A0A165BTX8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LAESUDRAFT_815724 {ECO:0000313|EMBL:KZT01645.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT01645.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT01645.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT01645.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV427661; KZT01645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165BTX8; -.
DR STRING; 1314785.A0A165BTX8; -.
DR InParanoid; A0A165BTX8; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000076871; 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:UP000076871};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 61..102
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 366..532
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 639..788
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1005
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 132174 MW; A74D1730CEE6D713 CRC64;
MSNASARTPS PALSMSSRSS TPEVPVQPDH FYGAQHLPPS PDSDGRTWLD PEDDPLAQRG
IPVFKPTMEE FRDFEGYLNK VECWGMKSGI VKVIPPKEWT DALPPLTEPL AQVKLKNPIE
QYMLGRGGLF RQENIEKRRI MSVREWAELC AKEEMRAPGI DDIGLHARST NGSAKPRTRR
ARRKRESETA EPEHAIKAEE EEEEISPYLA HPHDQGRESL ASPPNSVAAV DTPAADGENV
GAPTPAPQAT GVDENVRIGF SDNGDPHHEP GEDARHDEEE EEKPRSKGKR ATQTREAREA
NLAERAAKDK AFLETFDPHS DWLPPNTTPF DYTVDFCREL ERRYWRNCGL GKPAWYGADM
QGSLFTDETK EWNVAHLESA LSRLLPASSK GLPGVNTPYL YFGMWRATFA WHVEDMDLFS
INYVHFGAPK YWYAVPQARA TALEQTMRGY FPKDVSHCSQ FLRHKSFFAS PKLLSSSSCR
PNTLVQCAGE FVITFPMGYH AGFNLGFNCA ESVNFALESW LDLGRKAKAC DCVNFSVRID
VDRLLLEREE EERAKLEADK PRRPKTKPKP GKNSESKSQG KRKTEAPESP SKLKKPKTAR
PSKGKQSNSS AEGSQASQSK VAPAKVTLKL PPKPKEPEAF PCCLCVSMDK EKLLRVHDPP
LWRTDDEVAQ ESAGTETIWM AHEVCANVIP ETWVDEVEVG EVGQDGTRAK ERVVFGVDGI
VKDRWNLRCS ACTRTRYRAH GAPIQCTKGK CPKAFHVSCA REGASHNIVY KELREVEKEV
VLLIPQVGAA ATKPNQVAPT GGEQAALVPM EGNIDVQSDA TSVSLEPSAP TVLKLIRKLE
VQVLCSQHNP AVAEAKKLLK QDKIRKELLA LPPMSRIKLR VSAGVFEVSL LRVIEETGSV
EVLWDRGFRK EFKWGSVVFG NTDGLTIGQK PAEPAAEPEQ YVPRPIQPRP VWPSYSAAPP
VMDYRYQMHA STSTPPVAGS GMSSPAPSTS ASQAYPPPPS YPSYGPNYQY KPTTWRYQQY
PVSNSGSQYG AAGPSTAVSY PYSPSAYQPS TYQPYSGYNF QMQPQTQPAQ QHSPAQLAQQ
AEQLQPSQSI PQLQQPEPQS EPEPQPQVQQ LKPSQLRSLQ WQRPYMGPKA ILPAPSVARP
PISQTVPYHL HGQSQQSWQT GYATPTAANA APSPAPAEPD PSPMQQAAPA NATS
//
