ID G0RZ57_CHATD Unreviewed; 1548 AA.
AC G0RZ57;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=CTHT_0001780 {ECO:0000313|EMBL:EGS23485.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS23485.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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; GL988032; EGS23485.1; -; Genomic_DNA.
DR RefSeq; XP_006690727.1; XM_006690664.1.
DR STRING; 759272.G0RZ57; -.
DR GeneID; 18254216; -.
DR KEGG; cthr:CTHT_0001780; -.
DR eggNOG; KOG0955; Eukaryota.
DR eggNOG; KOG0958; Eukaryota.
DR HOGENOM; CLU_001442_4_2_1; -.
DR OMA; PWGGFTN; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000008066; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 133..174
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 399..562
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 654..777
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 84..127
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 15..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..610
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..990
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1548 AA; 170592 MW; 3562C5C1AD9514F6 CRC64;
MSIEAIGATA PTAALDAKLS SSSDSGSSSK DLGLNSPPDS NGADAMDVDN SDSELSDLDD
IASKLDGVIG DLDIEQKCQE VESAEKMEVE KAVLIEAKDD ATKEDANKEA QKEIEEEEED
IGEIEPDHWT GGVPVFKPSY RQFKDFKRFM EAVDKYGMQS GIIKIVAPEE WKNSLPPIDD
LIKRIRVRDP IKQEIMGHNG TYRQINILHQ RTYTLKQWKQ LCDQSEHQPP ARRGERRANA
DQKPPRTRAA VAAAAATAAG PSRPVTRSTA AATPTKKGRG CRVTRQSAKL AKHDDEELEE
RPMTPVSPEA EKEEVLDSIG QEAEEAKEGG AIARRKRTAR GRREGSVVID EEHFKDFDYN
MDISDFTPER CEELEKIYWK TLTYAPPMYG ADLPGTLFDE SVEIWNLNKL PNLLDVLGTK
VPGVNTAYLY LGMWKATFAW HLEDVDLYSI NYLHFGAPKQ WYSIPQKDAR RFEAAMKSIW
PQEAKACDQF LRHKGFLISP SHLKQHYNIT VNKCLSYPGE FVVTYPYGYH SGFNLGYNCA
EAVNFALDTW LPMGKIAKKC ECAQAQDSVW VDAWEIERKL RGEESEYEET EDEEDEVDEV
GDEDEEVETG LPSPPSDHTA KVKLPRRKRK RAEGEEAEPR VKKKIRVRQK PHAEQPCCLC
PNDIPGAEIL DTDDGRKAHR MCGLYIPETY VETVGGKEII ANVANIDKAR LELKCLYCRS
KKGACFQCSH KKCPRAYHAT CAAAAGVFVE EGEVPVFGED GTEYKEQAFE FSCRFHRTKR
DRKFEGDALE NDPEIRKAAK ALKKNDICQL QFYRGDIFAG VVVENHLDEE TLLIDVIPNG
DRVEVEWKWL LLPDPADFRL PKASPNAIPL PTCRKAQKAI NAKRTDDEVP RKDEEFGPGY
VWAEFSTCEP FRNRAQTKVD LSKENQIWYY LGETSTDAKA QYTENPAIKR HNPKSNFLES
LPKPVVAPTP ILGAPPPPPP PPPPPPPQQQ QQQQQQTGDV LALKQEKPYL YKPKIPVAPA
AGTQAGYATQ TFTSVPASGP FPPQPSPAQA NKPSTMSMYH HHGSPQGGQK EQPQQQQCPP
NMQYQQPPQQ PKNSSSLFSS TDRFAPVGGS NGFPTLPGLT WPPAHMKSGH HHHPQQQHYG
LQQPQSRVGV AQTTANMPPL VPMTSSHLQP QYGAQQQVPG GAQQQQPQPA MCAYQKYSFF
QLNHNRDPSR YRTPYGQWGG FVNGYEGNLR EFLLRAQKAL NGGSSSKGPK PLVSAQTTGY
PQTLPRPQQP QQSVLAPAPA PASAQQAGGQ PLHPAIRMPY GVAPAQAQSQ AQVPIAPSPT
PMQAPAPAPA SVPAKEKIKQ PFHKQSTSPI PLPPYVREMQ MAAKAAQQGK AGAQATTQQP
STSVPASNQA QIQPASAAAT TSTPQPALPQ SPVQTPTSTT ASPTQEKAQP NQASSSAAAA
TQNTPPQTHP QAYPSPPESK EPGQQGQRDT DVDKSRSVST MELTAASGIE VEQKQEGQVQ
GRQLAQEDSQ ALVQKMMINL RRASLSLVEE ADGQVSAIGS GAEDAASS
//
