ID A0A4U6XQC5_9PEZI Unreviewed; 1646 AA.
AC A0A4U6XQC5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 02-APR-2025, entry version 18.
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 Name=RPH1 {ECO:0000313|EMBL:TKW58043.1};
GN ORFNames=CTA1_779 {ECO:0000313|EMBL:TKW58043.1};
OS Colletotrichum tanaceti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=1306861 {ECO:0000313|EMBL:TKW58043.1, ECO:0000313|Proteomes:UP000310108};
RN [1] {ECO:0000313|EMBL:TKW58043.1, ECO:0000313|Proteomes:UP000310108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP57314 {ECO:0000313|EMBL:TKW58043.1};
RX PubMed=31150449; DOI=10.1371/journal.pone.0212248;
RA Lelwala R.V., Korhonen P.K., Young N.D., Scott J.B., Ades P.A.,
RA Gasser R.B., Taylor P.W.J.;
RT "Comparative genome analysis indicates high evolutionary potential of
RT pathogenicity genes in Colletotrichum tanaceti.";
RL PLoS ONE 14:e0212248-e0212248(2019).
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:TKW58043.1}.
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DR EMBL; PJEX01000031; TKW58043.1; -; Genomic_DNA.
DR STRING; 1306861.A0A4U6XQC5; -.
DR Proteomes; UP000310108; 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:UP000310108};
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..94
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..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..72
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 273..284
FT /note="Basic and 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 861..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1333
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1383
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1400
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1574
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1585
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1603
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1646 AA; 181643 MW; 5BBA4E98DE7F853E CRC64;
MMSTDAVSAP VPEPVTVPAQ STTTADHDQE EPALGQIECA KPAFLHSPPD SNNAHKSEAS
DSELSDLDED AVDPSANATA KQDEPPVEDD IGEVLPDHWS GTVPVFKPTM HQFKDFKLFM
TKVDKFGMKS GIVKIIPPSE WKESLPRLDD LVKQIRVREP IKQDIMGSNG TYRQVNILHQ
RSYNLPQWRQ LCDQSEHQPP ARRGERRANV EKPKPRSAPR PRAEAKSTAS GSKKKGRGRP
RRGKAKAKGQ DEDEEDDVQD DEKRPMTPVS PKPDADVEVK 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 EDEDDEEDED EDDDDATGLP
SPPDSNGVVK PARKRKRAAG DKDGKTKVKK IRLKVKTRAE PICCLCPSDI PGAEILPTDD
GRKAHRMCAL YLPETYIDTV DDKEIIANIA NINKERLDLK CLYCRSKKGA CFQCSQKKCA
RAYHATCAAA AGVFVEEAEV PVFGEDGTEY KEQAFEFSCR FHRTKRDRKY DGDALEEDTR
IREAASALNK GEICQLQYFK GEIFAGVVVE NRSEEQTLLL DIIPNGDRLE VEWKWLLLPD
PSDYHLPKAS ARAIPMPSSQ KAKDQLNAKR PADETPRKDA PFVEGFTWAE FHPCNECANP
NQDKVDLSKD NQLWHYLGKT STEAKAQYSE EPSKELHNPK SNFLDTIPKP PKPVSASTAH
RRVSNLPPQQ SPMFVPGPTD QTGPKSEKPY VYKPRKPVQT NYAGTGSFTT QTFALTASPS
PSPMGQQLHF GSDPRHPTTG AQFAQQRSTP DSHRQHVPRF SPAGQGYYQS PDAVQRASPY
STAGSQSAGG GGRPAQQTWA MPSQNPKPLL PHGNSHGSSQ QTHRRYSVAH TPSVAMKDSK
TYRTPYAPWG GFTNGYEGNL RAHLMRTSPE AFFKNRQGSV QGGTSTATPP AGPQASAYGG
PYHNTLTSTK PQGSIGMYGV KTTAPSHSSP AQQAPQNNAG RQYPASMSPS PAANVAQLMP
NGHGNGWHMQ QPQSTPLHPA IRPQYGTWPN QPNQLQQPAQ FLPQAAQQQF SQPPSQQQTP
QQPVASQPQQ NQAKTQPVAK PAAPKVQYKI PEKQTPVPLP AKYLAAIGKL PSATTTSRTS
SQSGAKLQGT ASLSSASSSA EVTNRIAPAT DAHAPPTESS ADPHSPANSN GPMAQAAPRA
SQTPVPVPYA PAPASNSRMP FTNQSSTVAF PRQAFQPIQP TPHRTQVCTA PSSQHLCQPM
SQPPRAEHHI LNPAEILAQI ATQPRMNPPT PTTPSHQSMQ SPVSQATAVP PYQHHGSGWG
VMQQGQQSQG YASHQHQHQH QHQHQHQSQP PQHQHQNQPG PMQSGTPHCP SPQVAGGEVP
LPEVPADSTA LVERMMQNLR RAAFQG
//
