ID A0A8T9BIH9_9HELO Unreviewed; 1408 AA.
AC A0A8T9BIH9;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 10.
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:TVY19910.1};
GN ORFNames=LARI1_G002921 {ECO:0000313|EMBL:TVY19910.1};
OS Lachnellula arida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Lachnaceae; Lachnellula.
OX NCBI_TaxID=1316785 {ECO:0000313|EMBL:TVY19910.1, ECO:0000313|Proteomes:UP000469559};
RN [1] {ECO:0000313|EMBL:TVY19910.1, ECO:0000313|Proteomes:UP000469559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 203.66 {ECO:0000313|EMBL:TVY19910.1,
RC ECO:0000313|Proteomes:UP000469559};
RA Giroux E., Bilodeau G.;
RT "Whole genome sequencing for identification of molecular markers to develop
RT diagnostic detection tools for the regulated plant pathogen Lachnellula
RT willkommii.";
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:TVY19910.1}.
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DR EMBL; QGMF01000080; TVY19910.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000469559; 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:UP000469559};
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..54
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 517..571
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 874..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Low complexity"
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 184..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..536
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..570
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..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1024
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1231
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1328
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1408 AA; 157751 MW; 4094579DDE4AE33E CRC64;
MSDDTVVVAA APGPAPEVNG LHSPPDSNMK DASDSELSDL DEEQPEQPGL ANDDIGEIEP
AYYSDDGVPV FLPSMEQFKD FTRFMTKITK YGMRSGIVKV IPPPEWKAAQ PRLDEAVKTI
RVKEPIKQDI MGTSGTYRQA NIVHQRSYNL PQWRQLCDQS DHQPPAKRGE RRANQDKQAK
PIPKTRSTAT PSSSASKGRG RGRPPKGKAS RNSTVEKEDE GQATPDRLPT PVSPLMKPEE
DNETVKLDQE DVDESPSKPK FGSRQAKAIS VSSRRKNNRR EVAGKIDEAA FVDFKYELEE
EFPPERCEDL ERSYWKTLTY APPLYGADMP GTLFTDQTTS WNLGKLDNIL DVMGSKIPGV
NTAYLYLGMW KATFAWHLED VDLYSINYLH FGAPKQWYSI AQGDARRFEA AMKTIWPTDA
KACDQFLRHK TFLISPQHLL SNFNIKVNKI VAHPGEFVIT FPYGYHSGYN LGYNCAEAVN
FGLEEWLEYG RVAKKCDCDQ AQDSVWINVH ELERKMRGEE TEYEETDEED EEEEEGGLPT
PPDSNGDSKL KIPKKKRKRS ANDKSGNDHI KRVRIRIKAP SKEPCILCPN DIPSEDLLPT
EEIGSKVHRI CAMYIPETSV DEDNTKEFVT DVKYIDKARL ELKCNYCRSK KGACFQCSQK
KCTRAYHATC AAAAGVEVQQ GEVPRFGEDG TEYKEWGIEF SCRFHRTKRD KKFDGDALEN
DGRLREGGAE LKIGEVCQAQ YYRGDIFAGA VVENRRSEET VLLDILPRGE RVEVEYKWLL
IPDPADYHLD KPSANAIPMP KSRKDKQSLN TSRRQADDNP RRDDPFVEGH TWAEFKMEEI
ARNVAQCKVN FAKEGQLWHY LGRNSTEARA QFTEDLAKPR NNPKANFLDT LPRATAPTIP
RHSYSASYPT KTSHPSPNVS RAPSRPPLPP SNKSEKPYAY KPRDIGDTYR VDQQAYRSQQ
SFLQQSAPSV PPSVPYSFGT DPRYQTAQPN RPNQYSRPAS GSPLAPPPVG PLAPPTQYRP
PHPAAMPSRP SNPFTGRAPQ NSRPSKPNPF ANYTYLQKEH NRSPLEYKSP YRPGGGFMNG
YQGNLGQHLQ QTLFQKRSGS AAQNSTLYTS ARAPYIAGQP SPTVGSYSPS NAAPYANYGG
TTASQKQPPA PGGMPTAAQN SWERRDTQLH AAIRQEYTQS PMFHQHYQPP RQPTQYQGSA
VLQPPPMWNR QAYQPGQMPQ GNQAPPQQNQ GYSQAPYSQA PRPQQPHVTQ PQSYHTSPGP
QTSNASWQSK QFPKPAESQN AAPSYQPPQY QPSNPGTQSS PHNMYAPSQP QGQYRPSSSH
QSAQPLSSIA QKASQSPTSH GQSSPTLQDQ ENKAVYPHQQ YFQKPQAQVP QPYAHAPQKY
EPADVPVDST SIIEKIMLNL KGAKPANV
//
