ID A0AAD8V875_9PEZI Unreviewed; 1641 AA.
AC A0AAD8V875;
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=LY79DRAFT_508888 {ECO:0000313|EMBL:KAK1596644.1};
OS Colletotrichum navitas.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=681940 {ECO:0000313|EMBL:KAK1596644.1, ECO:0000313|Proteomes:UP001230504};
RN [1] {ECO:0000313|EMBL:KAK1596644.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 125086 {ECO:0000313|EMBL:KAK1596644.1};
RG DOE Joint Genome Institute;
RA Baroncelli R., Diaz J.F., Benocci T., Peng M., Battaglia E., Haridas S.,
RA Andreopoulos W., Labutti K., Pangilinan J., Floch G.L., Makela M.R.,
RA Henrissat B., Grigoriev I.V., Crouch J.A., De Vries R.P., Sukno S.A.,
RA Thon M.R.;
RT "Comparative genomics, transcriptomics and evolutionary studies reveal
RT genomic signatures of adaptation to plant cell wall in hemibiotrophic
RT fungi.";
RL Submitted (JUN-2021) 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:KAK1596644.1}.
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DR EMBL; JAHLJV010000011; KAK1596644.1; -; Genomic_DNA.
DR RefSeq; XP_060417497.1; XM_060553996.1.
DR GeneID; 85438236; -.
DR Proteomes; UP001230504; 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:UP001230504};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 101..142
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 387..550
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 639..762
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1518..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 200..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..245
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..299
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..595
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1339
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1438
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1572
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1593
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1641 AA; 181480 MW; 885F9FEB310406B4 CRC64;
MMSTDAASAP VPEPVTVPAQ PAKTADHDQE EPALGQIECA KPAFLHSPPN SNNAHKSEAS
DSELSDLDEE AVDPSATAKE DEAPVEDDIG EVLPDHWSGT VPVFKPTMHQ FKDFKLFMTK
VDHYGMKSGI VKIIPPSEWK ESLPRLDDLV KQIRVREPIK QDIMGSNGTY RQVNILHQRS
YNLPQWRQLC DQSEHQPPAR RGERRANVEK PKPRSAARPR AEAKSSSSGS KKKGRGRPRR
GKAKGKSQDE ENDEQEDEKR PMTPISPKPD VDVEVKKEEL VNSVEDPGMD VDEEEEEEEP
RVLGRMGRMG GVRPAKPKTQ SVSARRKYSK REGSAMIDEK AFEDFDYQMD VSDYTPERCE
ELERIYWKTL TYAPPLYGAD LMGTLFHEST EIWNLNKLPN LLDVLGTKVP GVNTAYLYLG
MWKATFAWHL EDVDLYSINY LHFGAPKQWY SISQADARRF EAAMKNIWPT DAKACDQFLR
HKGFLISPSH LKQHYNITVN KCVSYPGEFV VTYPYGYHSG YNLGYNCAEA VNFALDSWLP
MGKIAKRCEC AQAQDSVWVD VYDIERKLRG EPTPEYEETE DEEDEEDEDE DEDDATGLPS
PPDSNGVIKP ARKRKRATGD KDGERKVKKI RLKVKTRAEP ICCLCPNDIP GAEILPTDDG
RKAHRMCALY LPETYIDTVD DKEVIANVAH ISKERLDLKC LYCRSKKGAC FQCSQKKCAR
AYHATCAAAA GVFVEEAEVP VFGEDGTEYK EQAFEFSCRF HRTKRDRKYD GDALEDDTRV
RDGAATLKKG EICQLQYFKG DIFAGVVVEN RSDEQMLLLD IIPNGDRLEV EWKWLLLPDP
SDFHLPKASP KAIPMPSSQK AKDQLNAKRP ADEIPRKDAP FVEGYTWAEF HPCAECANPN
QAKVDLAKDN QVWHYLGKTS TEAKAQYSED PVKELHNPKS NFLDTIPKPP KPVTANTTHR
RVSAIPSQPP PVAAPGPVVQ NEFKSEKPYV YKPRKPLETH YAGAESFATQ KLTPTASPSP
SPMGQQLHFG SDPRYPTAGP PFVQQKYMPD VHQQYVPRAN PAGQGYHQSP NAMPRVSPYI
TPGSQPAGGV RTTQQTWATP TQSSKPQLPH GGSHGSGQQT HRRYSAAPTP SVAMKDSKTY
RTPYAPWGGF TNGYEGNLRA HLMRTSPEAF FKNRQGSIQG GASTPNPPAR PQATGYSGPY
FNTLTNTMPQ GSVDMYGVKT TAPSYLSPAQ QASQDSARLQ YSASMSPSPV ANGAQSASNG
HGNAWRTQQS QSTPLHPAIR PQYGTWTNQP QHSAQSPSQP AQQQFPQPLS QQSHPAASAT
QPPLNQAKPQ AAAKPAAPKV QYKIPEKQTP VPLPAKYLAA MGKLPSAATP SKASSQKTEA
KSQDVGPSQT SGPAEDFARG TPAPNSQNHS SQVNPPSQSA TTSNGSMIQQ APQVSQTPVP
VPDTPVPTST SRMPFTNQSL TTAFPRQPAQ LNQPPYNHNQ AFTTPSVHQH FSGPVRQPPS
EHHALNPAEI LAQIATQPRM NPPTPTTHSH QSMPSPAPQA TGVPPYQNHG SCWGAAQQAR
QQPAYQPQGY APSPGQHAEP VQHQNQTQYQ QHQSGPMQNT APNHASQRAP EGEVPLPEVP
ADSTALVERM MQNLRRAAFQ G
//
