ID A0A8H8RIV0_9HELO Unreviewed; 944 AA.
AC A0A8H8RIV0;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
DE Flags: Fragment;
GN Name=RPH1 {ECO:0000313|EMBL:TVY34832.1};
GN ORFNames=LSUB1_G008238 {ECO:0000313|EMBL:TVY34832.1};
OS Lachnellula subtilissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Lachnaceae; Lachnellula.
OX NCBI_TaxID=602034 {ECO:0000313|EMBL:TVY34832.1, ECO:0000313|Proteomes:UP000462212};
RN [1] {ECO:0000313|EMBL:TVY34832.1, ECO:0000313|Proteomes:UP000462212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 197.66 {ECO:0000313|EMBL:TVY34832.1,
RC ECO:0000313|Proteomes:UP000462212};
RA Giroux E., Bilodeau G.;
RT "Genome sequencing and assembly of the regulated plant pathogen Lachnellula
RT willkommii and related sister species for the development of diagnostic
RT species identification markers.";
RL Submitted (MAY-2018) 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:TVY34832.1}.
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DR EMBL; QGMJ01000594; TVY34832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8H8RIV0; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000462212; 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:UP000462212};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 68..109
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 335..498
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 582..706
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..45
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..197
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..209
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..537
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 944
FT /evidence="ECO:0000313|EMBL:TVY34832.1"
SQ SEQUENCE 944 AA; 106777 MW; 87A477705D50BA8C CRC64;
MSDDTVVVAA APGPALEANG LHSPPDSNMK DASDSELSDL DEEQPEQPAP ASDDIGEIEP
SYYSDDGVPV FTPTMYQFKD FTRFMKKITK YGMRSGIVKV IPPPEWKAAQ PRLDEAVKTM
RIKEPIKQDI MGTSGTYRQA NIVHQRSYTL PQWRQLCDQS DHQPPAKRGE RRANQDKHIK
PAPKTRSTTA PSSSASKGRG RGRPPKGKAS RNSTVEKEEE GQATPDRLPT PVSPSMKPEE
DNETVKLDQE YADESPSKPK FGSRQAKAIS VSSRRKNNRR EVAGKIDEAA FVDFNYELDE
EYPPERCEDL ERSYWKTLTY APPLYGADMP GTLFTDETTS WNLGKLDNIL DVMGSKIPGV
NTAYLYLGMW KATFAWHLED VDLYSINYIH FGAPKQWYSI AQGDARRFEA AMKTIWPTDA
KACDQFLRHK TFLISPAHLL SNFNIKVNKI VAHPGEFVIT FPYGYHSGYN LGYNCAEAVN
FGLEEWLEYG RVAKKCDCDQ AQDSVWINVH ELERKMRGEE TEYEETDEED EEEEDDSLPT
PPGSNGDSKP KILQKKRKRS ANDKSGNENI KRVRIRIKAP SKEPCILCPN DIPSEDLLPT
EEIGSKAHRI CAMYIPETSV DEDNTKEFVT DVKYIDKARL ELKCNYCRSK KGACFQCSQK
KCTRAYHATC AAAAGVSVQQ GEVPRFGEDG TEYKEWGIEF SCRFHRTKRD KKVDGDALES
DERLRKGGAE LKIGEVCQAQ YYRGDIFAGA VVENRRSEET VLLDILPRGD RVEVEYKWLL
IPDPADYHLD KPSANAIPMP KSRKDKQSLN TSKRQADDNP RRDDPFVEGH TWAEFKMEEI
ARNVAQRKVN LAKEGELWHY LGRNSTEARA QFTEDPAKPR NNPKANFLDT LPRAIPQALP
RHSYSASYPS KTSHPSPNVS RAPSRPLPPS SNKSDKPYAY KPRE
//
