ID B6Q8E0_TALMQ Unreviewed; 1395 AA.
AC B6Q8E0;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=PMAA_068390 {ECO:0000313|EMBL:EEA25744.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA25744.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995900; EEA25744.1; -; Genomic_DNA.
DR RefSeq; XP_002146291.1; XM_002146255.1.
DR STRING; 441960.B6Q8E0; -.
DR VEuPathDB; FungiDB:PMAA_068390; -.
DR HOGENOM; CLU_001442_1_3_1; -.
DR OrthoDB; 48111at2759; -.
DR PhylomeDB; B6Q8E0; -.
DR Proteomes; UP000001294; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 78..119
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 343..506
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 587..712
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1395 AA; 156767 MW; 83E42993CE087F2B CRC64;
MTTALDQQAP APALESFHSV ETNAASITPP NSADGKKNVS EGVPSELSDL DLDHNAAASV
EVVEEDIEPD HYYEGGRIPV FKPTMDQFRD FQAFIQKIDK YGMKSGIVKV IPPQEWRDAL
PPLDEAVKSI RVKNPIMQEF HGAHGTYTQA NIEKQRSYNL PQWKALCDDG SHQPPARRGE
RRRTQEKAAR APVVKTQTTT ARSGSQKRGP GRPPKRTREV KIKEESPADD RSEKSRLEGP
PTPVSPESNP VETKTEDLSD GEALPAAKRR GRQPKSVSAR RKHNRGETLD QVDEEAFKDF
DYRIHDNDEY TAERCDELET AYWKSLMFNN PMYGADMPGS LFDDSTTSWN VAKLPNLLDV
IGQKVPGVNT AYLYLGMWKA TFAWHLEDVD LYSINYIHFG APKQWYSISQ EDAPRFEAAM
KSFWPSDAKN CDQFLRHKTY LVSPSILKSR FGITVNKVVH YEGEFMITYP YGYHSGFNLG
YNCAESVNFA TEQWLDYGRI AKKCNCESDS VWIDIGDIER KLRGEPTPEY YDDDEIDSDL
SDEDGASDLL TPPRSVPEKS TRGRKRKLEG DEPRSKRARM QNHTIRKIPC VLCPNDMDYE
DLLPTEDGKS HAHRRCATYI EETSILRDDS GREVVCDIDK IPKARMGLKC LFCREVRGAC
FQCNFGKCTR AYHPTCALLA GVQVEFGSIL VIADSGQQYY VPSVDLKCKY HRQKRLGPSE
TPDEDRKVLQ AASRLSMGDL LQFQADKEIN GAVVLENRPI ERMLKLKVLP RGDVIELPYR
WILVVRKTNF APLPPGTQPL PAHLVRKAET HRDLSNTVPQ PGTPFFDANA PFQWAEFETA
SLPADAIRVR VDIAGNKPEQ IWYYLGETST ECRAQFTHNP SVTVHNARSN FLEMMKPLPV
SALSAGRFRQ PPSLPQTPQS ARSNPHHLTA PPNTTLPSSS SSLQRRSPNT AMTPAYRHLP
PQHHLNLSHF NHAAANVTSI YAAANAAVRP NPYAAFPKPQ PDPPANTFAN VRELIARRRL
AQMTDHANVL AGYKIVSSEL VVETLLGPMG SVPPDNGMEK LELAMAQQRV QPRALDGSLL
PLQPLNMRSE EVTTLLRMLR FSVVTYRDRL DVIVKKEPDY IKQEPFDRPN YGRVAGRFAY
LEQQAAQTPA VYKSPYESPF GVAEWAKKEY NLVEEEPFSK PSLANDYFAS LSPADQEKIV
KACGSWVQER IVERAPSHSR QSSTSNFRLS AALAQQNHSN NNNPTIDITA VDDLPMNGMD
RMDRLDRLDF PLHADSPTSS FSRPHLVGFP SPHDFNSHGD HESSIVPRHL SDHHDLFGDQ
QANTRFWQHG PWGPGGDGTT PIEENRPFFG PHERLKHDYA SSELSLGRGP SSLHSVDMAG
FGMDTTEDLC EILSP
//
