ID A0A135V6T5_9PEZI Unreviewed; 1608 AA.
AC A0A135V6T5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 02-APR-2025, entry version 27.
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=CSAL01_04960 {ECO:0000313|EMBL:KXH68454.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH68454.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH68454.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH68454.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) 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:KXH68454.1}.
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DR EMBL; JFFI01000304; KXH68454.1; -; Genomic_DNA.
DR STRING; 1209931.A0A135V6T5; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000070121; 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:UP000070121};
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 390..553
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 641..764
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..69
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..261
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..598
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1245
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1311
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1355
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1389
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1490
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1608 AA; 177780 MW; 4FB32D94E5830AFC CRC64;
MSTDAVSAPV SEPAPVPAQS TTGDHDEEPT LGQIECAKPA FLHSPPDSNN APKSEPSDSE
LSDLDDDAVD PSAAPTIQDE APPPPPPEDD IGEVLPDHWS GTVPVFRPTM HQFKDFKLFM
TKVDHYGMKS GIVKIIPPPE WKETLPRLDD LVKQIRVREP IKQDIMGSNG TYRQVNILHQ
RSYNLPQWRQ LCDQSEHQPP ARRGERRANV EKPRPRSAPK PRTEAKSTPA GSRKRGRGRP
RRGKAKGKNQ DDEDDVQEEQ EEEKRPMTPV SPKPAVDAHV KVKKEEVVNS VEDPGMDVDE
DEPPTVGRMG RMGGARQAKP KTQTVSARRK YSKREGSAMI DEKAFEDFDY QMDVSDYTPE
RCEELERIYW KTLTYAPPLY GADLMGTLFD ESTEMWNLNK LPNLLDVLGT KVPGVNTAYL
YLGMWKATFA WHLEDVDLYS INYLHFGAPK QWYSISQADA RRFEAAMKNI WPTDAKACDQ
FLRHKGFLIS PSHLKQHYNI TVNKCVSYPG EFVVTYPYGY HSGYNLGYNC AEAVNFALDS
WLPMGKIAKR CECAQAQDSV WVDVYDIERK LRGEPTPEYE ETDEEDDEDD DEEDEDDATG
LPSPPDSNGI KSARKRKRAA GDKEGKAKTK RIRLKVKTRA EPTCCLCPSD IPGAEVLPTD
DDRKAHRMCA LYLPETYIDT VDGKEVIANV ANINKERLDL KCLYCRSKKG ACFQCSQKKC
ARAYHATCAA AAGVFVEEAE VPVFGEDGTE YKEQAFEFSC RFHRTKRDRK HTGDSLEDDL
RIREAAAALT KGDICQLQYF KGDIFAGAVV ENRADEQMLL LDIIPNGYVS LDYLNKKGLT
RFSDRLEVEW KWLLLPDPSD YHLPKASSKA IPMPSSQKAK DRLNAKRPAD EIPRKDAPFV
EGYTWAEFHP CNDCSNPNQT KVDLSKDSQV WHYLGKTSTE AKAQYSDDPV KQLHNPKSNF
LDTIPKPPKP VSASTSHRRV SAIPPQPAPL PMFTPGVAVQ NGPKSEKPYV YKPRKPVETN
YAGTGSFTTQ KFTPKASAPP TPGGQQLHFG SDPRYPIPGT QFVQEKFAPD VHQQYVPRPA
PARQGYYPPP NTMQRPSPCS TPGSQPAVGA RPAPQTWSTP SQNPRPPLPH STSQGSTQQN
HRRYSAAPTP SVAMKYAFFQ VHHNRSEFSN PCKFFSNTYT LNRDSKTYRT PYAPWGGFTN
GYEGNLRAHL MRTSPEAFFK NRQGSVQGGT PTPAPNAGPQ GPAYGGPYHN TLINVMPQGS
IGMYGVKTAT PYSSPAPQIP QNHARTPSYS SISPSPVPSG SQPSSHGQSQ GWHAQQPQLS
PLHPAIRPQY GSWANQPQQQ HPQHPQPAQP QPSQQPVPQQ TPQQSPASQS QPSQVKPQSA
AKPAAPKVQY KIPEKQTPVP LPAKYLVAMG KMPTAATPSK ANSKSTGSSV RSTTPSPATG
PGKHATQATS TVAVNGSSAQ PNSLSQAPNT SAGPKAETAP PVAQAPVSVP HTPVPASNSR
MPFTNQSMTT AFPRQPMQPQ SQAYNTPSTQ PFPPASRPRT EHLNPAEILA QIATTPRMNP
PTPTASSHQS MPSPVPPRTA AMPGYQNHDS TALVERMMQN LRRAAFQG
//
