ID L8G9S4_PSED2 Unreviewed; 1520 AA.
AC L8G9S4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=GMDG_03467 {ECO:0000313|EMBL:ELR08791.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR08791.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) 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; GL573224; ELR08791.1; -; Genomic_DNA.
DR RefSeq; XP_012741883.1; XM_012886429.1.
DR STRING; 658429.L8G9S4; -.
DR VEuPathDB; FungiDB:GMDG_03467; -.
DR HOGENOM; CLU_001442_4_2_1; -.
DR InParanoid; L8G9S4; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000011064; 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:UP000011064};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 111..152
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 379..542
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 630..749
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 65..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1472..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..585
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..979
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1520 AA; 169465 MW; B57C16983248148A CRC64;
MSTDVIARVA PVLDDNAAKM AAGLFSPPDS KMRMAFEDSD SELSELDEEG YSIGALPKMG
EARELREVGE KKDAGEGVDE KKPDEVAGEK EPEVDDIGEV VPDHYADEGR VPVFKPTMHQ
FKDFQVYMGR INPYGMQSGI VKVVPPQEWL DNQPEPDEII KTIRVREPIK QDIMGTNGTY
RQMNLLHQRA YNLPEWRQLC DQTEHQPPAR RGEVRATQEK PRTSGRGKKE STPAGEKVAA
QPRKKNGRAS RKSLAQKDAD KDQKERLPTP TSPPIKPDDD ADAPNLEPLE QDEPPRKRMG
GGGRGGRGGK ATTVSSRRKY GRRETAGKID EAAFENFEYK MDISDYTPER CEELERAYWK
TLTYAPPLYG ADMLGSLFDE RTTTWNLGNL PNLLDVMGTK IPGVNTAYLY LGMWKATFAW
HLEDVDLYSI NYLHFGAPKH WYSISQRDAR KFEAAMKSIW PTDAKECDQF LRHKTFLISP
STLLKNYGIK ANKITHFPGE FMITFPYGYH SGFNMGYNCA EAVNFAMPSW LEMGRIAKKC
DCAQAQDSVW IDVAQIERKM RGEETDYEES DEEEEEEEED DNGPTDLPTP PESSGDAKLK
QPRRKRKRVV SDKDGVDRTK RIRIRMKVSN EPCCLCPNDI KTQPLIPTED GRKVHRLCAE
YTPETDIDEG IVYNVAAIGK DRLDLKCMFC HSRKGAKIQC SQRKCTRSYH ATCAAAAGMF
VETGEIPVFG EDGTEYKQRG VEFSCRFHRA KRDKKLDEYV LEEDEDISRA AMAVREGEIC
QFQFLKKEIF AGVVVENRTS EEVLLVDILP SGDRFEVQYK YILLPDPTDF HLPKPSDKAI
PMPRSRHAKD ALVTTKRHAD DLPRKDDAFV EGATWAEFSA FNTPRNPAQV KVDLSKERQV
MYYMGKTSTE AKAQYTADWT KPVYDTRCNF LETIPKPPPA PRASYPASYP RPSGRAINPS
RPAPPRPTSY KPILPPTYSQ PPRASVKSDK PYVYKPKVEQ YYADRQVNNS QLPYTEDPAQ
QYRQPQPYPY GTDPRWPPAD NRGQGPYVAP AQPRAPAAVQ NHYSGFSTPN PLQQANTHTP
LGPQTHQQAS QAKQTPNDSP LQKPTAKPHG HRSSSSSAFK FNDVFQKYPY LQKQHNKAPG
TYRSPYRQDM LGFCNGYEGD FRKHMEAQMR KDPRLLSQHL MQASTTSSSQ LAAQSKTAAA
ETPRKSYPAI LPPAREQYSS PAASYYPNGA AVASAMKQQQ VLQAQITKPV GMQWDKKEGG
LHPAIRAEYG SAGGVVQAYQ PVVNPPAQTR RESPILPPGY QRPQPQPQPQ PQPQQQTAPA
PAAGQWNAQY QQPPQQNHVA TPPLPQQPGS AHMSPAAQYY SRPPSRPQSS PLTQPALQPH
MNAAAENVPP TQSFSQSYSA PVKSFYSDTY HAVGVVGRKG GMPAPAPAAA VGVDAGVATP
VAVMSGTMLG PLPPQQAAVD RKLNILTGAP VAPADTEIPD TPGPMEGVQG GDIPEIDTDS
AGMMETLMRN LQRAARQGQV
//
