ID A0A7D8UKT5_9HELO Unreviewed; 1405 AA.
AC A0A7D8UKT5;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 02-APR-2025, 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};
GN Name=RPH1 {ECO:0000313|EMBL:TVY51287.1};
GN ORFNames=LCER1_G009261 {ECO:0000313|EMBL:TVY51287.1};
OS Lachnellula cervina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Lachnaceae; Lachnellula.
OX NCBI_TaxID=1316786 {ECO:0000313|EMBL:TVY51287.1, ECO:0000313|Proteomes:UP000481288};
RN [1] {ECO:0000313|EMBL:TVY51287.1, ECO:0000313|Proteomes:UP000481288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 625.97 {ECO:0000313|EMBL:TVY51287.1,
RC ECO:0000313|Proteomes:UP000481288};
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:TVY51287.1}.
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DR EMBL; QGMG01000856; TVY51287.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000481288; 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:UP000481288};
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..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..278
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 872..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1348
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 180..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..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 957..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..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 1032..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1405 AA; 157556 MW; F87012C0BDAA8629 CRC64;
MSDDTVVVAA APGPAPEVNG LHSPPDSNMK DASDSELSDL DEEQPEQSAL ANDDIGDIEP
SYYSDDGVPV FLPSMHQFKD FTQFMTKITK YGMRSGIVKV IPPPEWKAAQ PRLDEAVKTI
RVKEPIKQDI MGTSGTYRQA NIVHQRSYNL PQWRQLCEQS DHQPPAKRGE RRANQDKQAK
PTPKTRSTTA PSSSASKGRG RGRPPKGKSS RNSTVEKEDE GQATPDRLPT PVSPLMKPEE
DNETVKLDQE DVDESPSKPK FGSRQAKAIS VSSRRKNNRR DVAGKIDEAA FVDFKYELDE
EYPPERCEDL ERSYWKTLTY APPLYGADMP GTLFTDQTTS WNLGQLDNIL DVMGSKIPGV
NTAYLYLGMW KATFAWHLED VDLYSINYLH FGAPKQWYSI AQGDARRFEA AMKTIWPADA
KACDQFLRHK TFLISPSHLL SNFNIKVNKI VAHPGEFVIT FPYGYHSGYN LGYNCAEAVN
FGLEEWLEYG RVAKKCDCDQ AQDSVWINVH ELERKMRGEE TEYEETDEED EEEEEDSLPT
PPGSNGDSKP KIPKKKRKRS ANDKSGNDHI KRVRIRIKAP SKEPCILCPN DILSEDLLPT
EEIGSNVHRI CAMYIPETSV DEDNAKEFVT DVKYIDKARL ELKCNYCRSK KGACFQCSQK
KCTRAYHATC AAAAGVEVQQ GEVPRFGEDG TEYKEWGIEF SCRFHRTKRD KKFDGDALEN
DGRLREGGAE LKIGEVCQAQ YYRGDIFAGA VVENRRSEET VLLDILPRGD RVEVEYKWLL
IPDPADYHLD KPSANAIPMP KSRKDKQSLN TSRRQADDNP RRDDPFVEGH TWAEFKMEEI
ARNVAQCKVN FSKEGQLWHY LGRNSTEARA QFTEDPAKPR NNPKANFLDT LPRATAPTIP
RHSYSASYPT KTSNPSPNVS RAPSRPPLPP SNKSEKPYAY KPRDIGDTYR VDQQAYRSQQ
SFLQQSAPSV PPSIPYSFGT DPRYQTAEPN RPNQYSRPAS GSPLAPPPVG PLAPPAQYRP
PHPAAMPARP SNPFTGRAPQ NSRPSKPNPF ANYTYLQKEH NRSPLEYKSP YRPGGGFMNG
YQGNLGQHLQ QTLFQKRSGS TAQNSTLYTS PRAPYISGQP SPTVGSYAPS NAAPYANYGG
TTASQKQPPA PPPAAQNSWE RRDTHLHAAI RQEYTQSPMF HQHYQPPRQP TQYQGSAVLQ
PPPMWNRQAY QPGQMPQGNQ APPQQNRGYS QAPYSHAQRL QQPHVTQPQS YHTSPGPQTS
HASWQSRQFP KSAESQNAAP SYQPPQYQPS NPGTPSSPHN MYAPSQPQGQ YRPSSSYQSA
QPLSPIAQKA SQSPISHGQS SPTLQDQENK GLYPHQQYFQ KPQAHVPQPY AHAPQKYEPA
DVPVDSTSII EKIMLNLKGA KPANV
//
