ID A0AAD9EF46_9PEZI Unreviewed; 1633 AA.
AC A0AAD9EF46;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
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=CCHR01_14813 {ECO:0000313|EMBL:KAK1842551.1};
OS Colletotrichum chrysophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1836956 {ECO:0000313|EMBL:KAK1842551.1, ECO:0000313|Proteomes:UP001243330};
RN [1] {ECO:0000313|EMBL:KAK1842551.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M932 {ECO:0000313|EMBL:KAK1842551.1};
RA Baroncelli R.;
RT "Colletotrichum chrysophilum M932 genome sequence.";
RL Submitted (JAN-2023) 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:KAK1842551.1}.
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DR EMBL; JAQOWY010000407; KAK1842551.1; -; Genomic_DNA.
DR Proteomes; UP001243330; 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:UP001243330};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 96..137
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 375..538
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 625..748
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..238
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..581
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..612
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1098
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1209
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1338
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1431
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1543
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1633 AA; 180920 MW; DEB01C1E95E283ED CRC64;
MSTDAVSAPV PEPAPVPAQS TANGDKEEPT IECATKPAFL HSPPDSNNAP KSDGSDSELS
DLDDDAVEAP QKQDEAQPEV EDDIGEVLPD HWSGTVPVFK PTMHQFKDFK LFMTKVDKYG
MKSGIIKIIP PSEWKENLPK LDDLVKQIRV REPIKQDIMG SNGTYRQVNI VHGRSYNLPQ
WRQLCDQSEH QPPARRGERR ANVEKPKPRS APRPRPAAKS TPSGSKKRGR GRPARGKAKI
QEEEEANEEG NRPMTPVSPK ADAEVEIKKE EVVDSVEDPG TDVDDDEPPT VGRMGRMGGI
KPSKPKTQSV SARRKYSRRE GSAMIDEEAF KDFNYQMDVS DYTPERCEEL ERIYWKTLTY
APPLYGADLM GTLFDESTEM WNLNKLPNLL DVLGTKVPGV NTAYLYLGMW KATFAWHLED
VDLYSINYLH FGAPKQWYSI SQADARRFEA AMKNIWPTDA KACDQFLRHK GFLISPSHLK
QHYNITVNKC VSYPGEFVVT YPYGYHSGYN LGYNCAEAVN FALESWLPMG KIAKRCECAQ
AQDSVWVDVY DIERKLRGEE TEYEETDDDD DEEDEDEDED ASGLLSPPNS NTVVIKTSRK
RKRAGDKGGK TKVKKIRLKV KTRAEPICCL CPSDIPGAEI LPTDDGRKAH RMCALYLPET
YIDTVDDKEI IANVANINKE RLDLKCLYCR SKKGACFQCS QKKCARAYHA TCAAAAGVFV
EEAEVPVFGE DGTEYKEQAF EFSCRFHRTK RDRKFDGDSL EEDERIRKAA AALKKGEICQ
MQYYKGDIFA GVVVENRADE QMLLLDIVPN GYDSPVGVEK NRLTCTSDRL EVEWKWLLLP
DPSDYHLPKA SAKAIPMPSS QKAKDKLNAK RPADEVPRKD APFVEGYTWA EFHPCDECAN
PNQVKIDLSK DNQVWHYLGK TSTEAKAQYS EDPAKEQHNP KSNYLDTIPK PPKPVSATAA
QRRPSNIPPQ PIPMASPSVA IQSGLKTEKP YVYKPRKPVE PSYAGPGTFT TQKFTPKASP
SPSPMGQQLY FGSDPHYQMQ QGHYAQQRFT PNIHQPYNPA GPGQYAASNN TQRQSPYATP
VQPPGGPAKQ AQQMWPTPSQ SPRPPPPPAG YSQASTPQNH RRYSAAPSPS VAMKYAFFQV
HHNRDSKTYR TPYAPWRGFT NGYEGNLRAH LMRISPEAFF KNNRQGSVQS ASPASSSAGR
PPAPAHSSPY YNTFTTAAPQ GSIGVYGQKT TTPSYSSPVP RPTHDPARTQ YTSMSPSPVP
NGSHQSPHGY NNAWNAQQQP PSTPLHPVIR PQYGAWVNQP QQPQPHNQAT PPHHQQAQQQ
QQTPQQPTAP QPAASHSQSA EKKAEAAPKP AAPKVQYKIP EKQTPVPLPA KYLAAMGKMA
PTPTKASPQS NGAPSQDKSS PTSASANSTR TPQVVGTQNS SAQVSSPSRP STASKKTAVP
VSQTPVPLPQ TAVPAPPQRM PFTNQFSANR PSQPTYQPQT QAHTGQPNPR PFQSVGQPRT
EHHSLNPAEI LAQIATQPRM NPPTPTTPHQ PMPSAAPQQA PGPRYYAGQQ VPQAHNGVMP
QQQYFQHYAP APQGQYPPPQ PQYAHQYPPQ NTAPSYPPQP APAGDVPLPE VPADSTALVE
RMMQNLRRAA SNG
//
