ID A0A2J6QJP2_9HELO Unreviewed; 1391 AA.
AC A0A2J6QJP2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 02-APR-2025, entry version 21.
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=NA56DRAFT_667770 {ECO:0000313|EMBL:PMD26491.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD26491.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD26491.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD26491.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KZ613467; PMD26491.1; -; Genomic_DNA.
DR STRING; 1745343.A0A2J6QJP2; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000235672; 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:UP000235672};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 65..106
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 328..491
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 578..700
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..191
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..205
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..531
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1020
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1194
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1300
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1391 AA; 156411 MW; D4F36FC0AC96D188 CRC64;
MSTNAMAVPA PENQPVGLQS PPDSNSAPID NGSDSELSDL EPDPEPEPET SELNLKPDYY
SDGGVPVFRP SMEEFADFQR YMRGVNPYGM KSGIVKVIPP PEWVAAQPRL DEAIKTIRVK
EPIKQDIMGT GGTYRQANFM HQRSYNLPQW RQLCNQSEHQ PPAKRGERRM NQEKYMKPTP
KTKSSGTPSS GSKKKSSGRS NKGKGKSAIS EPIEGTSTPD RLPTPVSPTM KAEEDTVQIK
EEVDDACDTP TRTKGGRQPK AISVSARRKN NRSESAAVDE AAFKDFKYEL EGEDYSPERC
EELERAYWKT LTYASPLYGA DMPGTLFDDR TTTWNLGKLE NLLDVLGTKI PGVNTAYLYL
GMWKATFAWH LEDVDLYSIN YLHFGAPKQW YSISQGDARR FEAAMKTIWP VDAKACDQFL
RHKTFLISPA HLLANFNIKV NKITHHPGEF VITFPYGYHS GYNLGYNCAE AVNFALDSWL
EFGRVAKKCD CSQAQDSVWI NVHEIERKLR GEETEYEETD EEDEDEEDDL PNDLPTPPES
SGDTKLKVPR KKRKRPTNEK GDNLNVKRIR VRIRAPTREP CILCPNDIPS EPVLFTEDGQ
KAHRLCALYI PETSIESGEK DTVIDVKYID KARLELKCNY CRSRKGACFQ CSQKKCTRAY
HATCAAAAGV LVEQGEIPVF GEDGTEYKEW GIEFSCRFHR TKRDKKYDGD ALDDDERILK
AASELKIGEV CQMQYYKGDI FAGAVVENRK SEQMVLVDIL PRGDRAEVEY KWLLIPDPAD
YRLPKPSPNA KPMPKSYKDK ESLNTSKRQV DDIPRAEDPF VKGFTWAEFK NHKLLRNPAQ
IKVDLGKDNQ IWFYLGKTST EAKAQFTEDA AKPRHNPKGH FLDTIPKPTT TLPRQSYAAT
YPSGLSQSTL ATPRAPIRPP QSAVSSASRP EKPYVYKPRN TGDMYRVDPQ AYRSQQNFLQ
RSTPYSFGTD PRWRSTEPST TPQLPNAAPA TNFPQSSTTQ TPLAPPLQAP YRPTYTHTHT
PPVPPKANNP FSGRPQPSSS RSNPFAKYSY LQKEHNRSPL EYKSPYRPGG GFMNGYQGSL
QKHLQQTLFR SKSGPSTPLS NPMMSYGSNL RSPYTPSRSS PGPSYNAGIS TSYGGWGTPN
SQRQVQQPTM NNPTSNTWEK KDASQLHPAI RQEYNSMFNH QYQPPQRSPS SQHQGSVLQP
PAMYDRPQLH PTYLNHTPQA RPVQQSMPPA TAQDIEQQQD LHQSASQPPI SETIQLASST
QSTTSAPPYG QYYQALSSTV RQSPSNYPSS QPQQQPQSPA VIQSPVLVPQ PQYQAPPEVY
QDKPVYPHQQ YFQKPEAQFQ VPPQAKAQVL QSVVQQSQAR DFPDVPADST SIIEKMMRNL
KKAAPVTSTT I
//
