ID A0A1B7Y406_COLHI Unreviewed; 1711 AA.
AC A0A1B7Y406;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 08-OCT-2025, entry version 33.
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=CH63R_10869 {ECO:0000313|EMBL:OBR06749.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:OBR06749.1, ECO:0000313|Proteomes:UP000092177};
RN [1] {ECO:0000313|Proteomes:UP000092177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA Thon M.R., O'Connell R.J.;
RT "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT structure and association of transposable elements with secondary
RT metabolite gene clusters.";
RL BMC Genomics 18:667-667(2017).
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:OBR06749.1}.
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DR EMBL; LTAN01000007; OBR06749.1; -; Genomic_DNA.
DR RefSeq; XP_018155267.1; XM_018305843.1.
DR GeneID; 28869950; -.
DR KEGG; chig:CH63R_10869; -.
DR VEuPathDB; FungiDB:CH63R_10869; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000092177; 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:UP000092177};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 103..144
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 388..551
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 640..763
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..73
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..260
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..300
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..596
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1380
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1426
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1614
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1638
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1668
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1711 AA; 189065 MW; B305B3E7284CBBFA CRC64;
MMSTDAVSAP VPEPATVPAQ STTTADHDQE EPALGQIECA KPAFLHSPPD SNNAHKSEAS
DSELSDLDED DVDPSANATA KQDEPPVEDD IGEVLPDHWS GTVPIFKPTM HQFKDFKLFM
TKVDKFGMKS GIVKIIPPSE WKESLPRLDD LVKQIRVREP IKQDIMGSNG TYRQVNILHQ
RSYNLPQWRQ LCDQSEHQPP ARRGERRANV EKPKPRSAPR PRAEAKSTAS GSKKKGRGRP
RRGKAKAKGQ DEDEEDDAQD DEKRPMTPVS PNPDADVEVK KEEVVDSVED PGMDVDEDEE
PRSLGRMGRM GGARPAKPKT QTVSARRKYS KREGSAMIDE KAFEDFDYQM DVSDYTPERC
EELERIYWKT LTYAPPLYGA DLMGTLFHES TELWNLNKLP NLLDVLGTKV PGVNTAYLYL
GMWKATFAWH LEDVDLYSIN YLHFGAPKQW YSISQADARR FEAAMKNIWP TDAKACDQFL
RHKGFLISPS HLKQHYNITV NKCVSYPGEF VVTYPYGYHS GYNLGYNCAE AVNFALDSWL
PMGKIAKRCE CAQAQDSVWV DVYDIERKLR GEPTPEYEET EDEDDDEDED EDEDDATGLP
SPPDSNGVVK PARKRKRAAG DKDGKTKVKK IRLKIKTRAE PICCLCPSDI PGAEILPTDD
GRKAHRMCAL YLPETYIDTI DDKEIIANIA NINKERLDLK CLYCRSKKGA CFQCSQKKCA
RAYHATCAAA AGVFVEEAEV PVFGEDGTEY KEQAFEFSCR FHRTKRDRKY DGDALEDDTR
IREAAAALNK GEICQLQYFK GDIFAGVVVE NRSEEQTLLL DIIPNGYASS TVSNVLGLTR
TSDRLEVEWK WLLLPDPSDY HLPKASARAI SMPSSQKAKD QLNAKRPADE TPRKDAPFVE
GFTWAEFHPC NECVNPNQAK VNLSKDNQLW HYLGKTSTEA KAQYSEEPSR ELHNPKSNFL
DTIPKPPKPV SASTAHRRVS NLSPQQSPMF VPGPTTQIGP KSEKPYVYKP RKPVETNYAG
TGSFTIQRFA PTASPAPSPM GQQLHFGSDP RHPTTGAQFA QQRSTPDSHQ QHAPRISPSG
QGYYQSSNAV QRASPYSTPG SQSAGGGQPA QQTWATPSQN PKPLLPHVNS YGSSQQTHRR
YSVAHTPSVA MKYAFFQVHH NRSEPPPLCR VLNVTYAIPR DSKTYRTPYA PWGGFTNGYE
GNLRAHLMRT SPEVFFKNRQ GSVQGGTPTS NPPAGPQAPG YGGPYYNTLT NTISQGSIGM
YGVKTTTPSH SSPAQQAPQD NAGRQYPASM SPSPAANGPQ LMPNYHGNGW HMQQPQSTPL
HPAIRPQYGA WPNQPNQPQQ PAQSPSQAAQ QQFSQPSSQQ QTTQQPVASQ SQQSQAKTQP
VAKPAAPKVQ YKIPEKQTPV PLPAKYLAAM GKLPSTTTTS RASSQSGAKS QGTASASGSA
DVTNRIAPAI DAHASRTESS ALPHSPTNSN GPRAQAAPRA SQTPVPVPHA PAPASNSRMP
FTNQSSTVAF PRQSFQPIQS TPHHTQVCTA PSSQHLSQPM NQPRAEHHTL NPAEILAQIA
TQPRMNPPTP TTPSHQSMPS PVSQAAAVPP YQHHGSSWGV MQQGQQSQGQ QSQGYASTPG
QYSQSATHHH YQPQHQLHHP YQGQVQHQHQ HQYQPPQHQH QTQPGPMQSG TPHCPPPQVA
GGEVPLPEVP ADSTALVERM MQNLRRAAFQ G
//
