ID A0A066XDU1_COLSU Unreviewed; 1697 AA.
AC A0A066XDU1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 02-APR-2025, entry version 40.
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=CSUB01_01275 {ECO:0000313|EMBL:KDN67348.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN67348.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN67348.1}.
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DR EMBL; JMSE01000824; KDN67348.1; -; Genomic_DNA.
DR STRING; 1173701.A0A066XDU1; -.
DR eggNOG; KOG0958; Eukaryota.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_001442_4_0_1; -.
DR OMA; PWGGFTN; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000027238; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 100..141
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 385..548
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 637..760
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..71
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..241
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..592
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1276
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1368
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1469
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1615
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1649
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1697 AA; 187521 MW; AFEA08DC385CA92F CRC64;
MSTDAASAPA LEPVTVPAQP GKAADHDQEE PALGQIECAK PAFLHSPPDS NNAHKSEASD
SELSDLDEEA VDPSATAKEN EAPVEDDIGE ILPDHWSGTV PVFKPTMHQF KDFKLFMTKV
DHYGMKSGIV KIIPPLEWKE SLPRLDDLVK QIRVREPIKQ DIMGSNGTYR QVNILHQRSY
NLPQWRQLCD QSEHQPPARR GERRANVEKP KTRSAARPRA EAKSTSSGSK TKGRGRPRRG
TAKGNSQDEE DDVQGDEKRP MTPVSPKPDA DVEVKKEELV DSVEDPGMDV DAEEEEEPRA
LGRMGRMGGV RPAKPKTQTV SARRKYSKRE GSAMIDEKAF EDFDYQMDVS DYTPERCEEL
ERIYWKTLTY APPLYGADLM GTLFHESTEI WNLNKLPNLL DVLGTKVPGV NTAYLYLGMW
KATFAWHLED VDLYSINYLH FGAPKQWYSI SQADARRFEA AMKNIWPTDA KACDQFLRHK
GFLISPSHLK QHYNITVNKC VSYPGEFVVT YPYGYHSGYN LGYNCAEAVN FALDSWLPMG
KIAKRCECAQ AQDSVWVDVY DIERKLRGEP TPEYEETEDE EDDEDEDEDD NDATGLPSPP
DSNGVIKLTR KRKRATGDKN GMTKVKKIRL KVKTRAEPIC CLCPNDIPGA EILPTDDGRK
AHRMCALYLP ETYIDTVDDK EIIANVAHIS KERLDLKCLY CRSKKGACFQ CSQKKCARAY
HATCAAAAGV FVEEAEVPVF GEDGTEYKEQ AFEFSCRFHR TKRDRKYDGD ALEDDLRIRD
GAAALKKGEI CQLQYFKGDI FAGVVVENRS DEQMLLLDII PNGYASSISL NEPRLTQTSD
RLEVEWKWLL VPDPSDYHLP KASAKAIPMP SSQKAKDQLN AKRPADEIPR KDAPFVEGFT
WAEFHPCAEC ANPNQAKVDL AKDNQVWHYL GKTSTEAKAQ YSEDPTKELH NPKSNFLDTI
PKPPKPVSAN TTHRRVSNIL PQSSPVAAQG PICQNGPRQE KPYVYKPRKP VDTHYAGTGS
FTTQKFTPTA SPSPSPMGQQ LHFGSDPRYP AASPQFAQQR FTPDAHQQYV PRVNPAGHGY
HPSPNTMPKA SPYSTPVPQP AGGARPTQQT WATPSQSPKP QLPHGGSHGS GQHAHRKYSA
APTPSVAMKY AFFQVHHNRL ELYNSTALFN GTDTLPRDSK TYRTPYAPWG GFTNGYEGNL
RAHLMRTSPE AFFKNRQGSA QGGAQASNPP ARPQAPGYGG PYFNTLTNTM PQGSIGMYGV
KTTAPSYSSP AQQASQDNAR PQYSASMTPS PVANGAQSTS NGHGNTWHTQ QSQTTPLHPA
IRPQYGAWTN QSQHSAQSPS QPVQQQFSRP PSQQSTPSQP AASAIQPPMN QAKPQAVAKP
TTAKVQYKIP EKQTPVPLPA KYLAAMGKLP SAATPSKANS QTNGTKSQDV GPSPASSPAK
HSAHGTSASN SQNQSSQVNA SAQSATTSNG PMTQQAPRVS QTPVPVPHTP VPTSSSRMPF
TNQSSTTAFP RQPVQLDQAP HNHTQAFTTS SAHQHYTGPA RQPPSEHHTL NPAEILAQIA
TQPRMNPPTP TTPSHQSMPS PASQTTGVTS YQNHGSSWGV TQQTRQQQPA YQPQGYAPPP
GQYVQPIQHH HQSQYQQQQQ QYLSQQHHQP GPMQNTTPHY AASQAPEKEI PLPEVPADST
ALVERMMQNL RRAAFQG
//
