ID A0A8H6DTX8_COCSA Unreviewed; 1314 AA.
AC A0A8H6DTX8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
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=GGP41_009094 {ECO:0000313|EMBL:KAF5847859.1};
OS Cochliobolus sativus (Common root rot and spot blotch fungus) (Bipolaris
OS sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=45130 {ECO:0000313|EMBL:KAF5847859.1, ECO:0000313|Proteomes:UP000624244};
RN [1] {ECO:0000313|EMBL:KAF5847859.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang H.;
RT "Bipolaris sorokiniana Genome sequencing.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 2-
CC oxoglutarate + 2 O2 = N(6)-methyl-L-lysyl(9)-[histone H3] + 2
CC formaldehyde + 2 succinate + 2 CO2; 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:ARBA00049349};
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF5847859.1}.
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DR EMBL; WNKQ01000012; KAF5847859.1; -; Genomic_DNA.
DR Proteomes; UP000624244; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0051864; F:histone H3K36 demethylase activity; IEA:TreeGrafter.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR CDD; cd15571; ePHD; 1.
DR FunFam; 2.60.120.650:FF:000024; Putative jumonji family transcription factor; 1.
DR FunFam; 3.30.40.10:FF:000377; Putative jumonji family transcription factor; 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; IPR055500; DUF7072.
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:SF7; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF23258; DUF7072; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 68..109
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 340..503
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 597..720
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 155..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..56
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..214
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..540
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..570
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1163
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1314 AA; 147519 MW; 78DCF3BE6CCEE5C6 CRC64;
MEASQDVVPS VEAPPVPQDD ATNKPALTPP TSEDNDKRFE DMSSELSDID SDDGEDIEPD
HYFEGGKIPV FKPTMDQFRN FKRFIDKVDK YGMKSGIIKV IPPTEWRESL PDLTEAVKSI
KVKNPITQEF NGQHGIYTQA NIEKQRSYNL PEWRAVTDEP HHQPPAKRGE RRKAAPEVPS
RTRSTRAQVA PSRNDDASPT PRRGPGRPTR RRQVKKEPVD DDDDEKPMDV PPTPTSPGKE
EKRSSRRVKK EPQAATPTRA RGRQPKAADE KKSVSSRRLN NRGAIADHVD EAAFENFDYR
LPGLEEYTVE RCKELEDNYW KTINYGQPMY GADMPGSLFD DSTTSWNVAK LPNLLDVLGT
KVPGVNTAYL YLGMWKATFA WHLEDVDLYS INYIHFGAPK QWYSISQEDA RRFEAAMQTI
WPNDAKHCSQ FLRHKTYLIS PQRLERDFNI KVNRLVHYEG EFVITYPYGY HSGYNIGYNC
AESVNFANES WLSYGRIAKK CMCESDSVWV DVNEIERKLR GEPTPEYYEE TDDEEDEDDG
ADRLPSPPVS VAGKTKAKAS RKSTGNKRKR GKEDSKDSSR SKKLKRIRIR IRIPGRGMPC
ILCPNDVEYD DLLQTDNGMK AHRICADYTP ETYIVKKNDV EIVCNVTNIG KDRLELKCNY
CRSKRGAVFQ CSQKKCTRAF HATCAVAAGV QVDLGPMPTF DEEGTEYFYD GYDFRCRFHR
PKKRNNKTVD VEALEKDKYV MSYGKTLKPK DVIQFQYVGG EMYQIYGAQV VENRPGEQAV
LVDVLPDGDR VEVEWKYILK LHPDESQRLK PSANAKPLPE HLKESDASLD ITNRTDGVPE
MGDPFHDPNS EQKWAEWYTA PEVTQKLAKV DLSKEDQLWY YLGKLSTEAR PQYTENPAKP
RNNPKSNFLD TVKPPPPPVP AFHRASYPAS YPLKPAPIAV PPVQQYMPNG RPYSYKPKDP
VVAPFRSPVY NPDTRKNPNS PVAHQPNVSY DHRMPHGQYG QQSNQGYLSH RPLHASQQQL
QYHPYVPPQS YSTASWKAQP ATSGPVLSGV EKYAQAPPHA NVLPPYPYAQ NIRQSSYSHG
QVPSAARAYG PPGRQAQGPS NGRSPISSMP SNPSGPHKPP ILDHGIAPEW MPKPPMSRAS
GTPTTIAPKP AASTGSTPPQ GYYGPPPTGS SVPKPSAQFQ SSDAFQREMA RTTQTTEAPK
WEQMLKQLAT ATGSLSEPSV TAPSPQEPQS RYPPSGPRSS LSQDLPASKE ESESKKLSPT
QQEPLRPTPS PISDDGKADG KADNAASPDQ EKPAPEPSQP DSKVHGAETW HYSS
//
