ID A0A8H8U1A2_9HELO Unreviewed; 1411 AA.
AC A0A8H8U1A2;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 13.
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:TVY29833.1};
GN ORFNames=LHYA1_G002016 {ECO:0000313|EMBL:TVY29833.1};
OS Lachnellula hyalina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Lachnaceae; Lachnellula.
OX NCBI_TaxID=1316788 {ECO:0000313|EMBL:TVY29833.1, ECO:0000313|Proteomes:UP000431533};
RN [1] {ECO:0000313|EMBL:TVY29833.1, ECO:0000313|Proteomes:UP000431533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 185.66 {ECO:0000313|EMBL:TVY29833.1,
RC ECO:0000313|Proteomes:UP000431533};
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:TVY29833.1}.
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DR EMBL; QGMH01000014; TVY29833.1; -; Genomic_DNA.
DR RefSeq; XP_031008620.1; XM_031146994.1.
DR GeneID; 41982214; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000431533; 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; 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:UP000431533};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 68..120
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 346..509
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 593..717
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1330
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 178..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..220
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..548
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..940
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1038
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1206
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1262
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1330
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1411 AA; 158098 MW; 2FAE8224417650B8 CRC64;
MSDDTVVVAA APGPALEANG LHSPPDSNMK DASDSELSDL DEEQAEQPAP ASDDIGEIEP
SYYSDDGVPV FTPTMYQFKD FTRFSLIGKY AKLNQMKKIT KYGMRSGIVK VIPPPEWKAA
QPRLDEVVKT MRIKEPIKQD IMGTSGTYRQ ANIVHQRSYT LPQWRQLCDQ SDHQPPAKRG
ERRANQDKYM KPAPKTRNTT APSSSASKGR GRGRPPKGKA SRNSTVEKEE EGQATPDRLP
TPVSPLMKPE EDNETVKLDQ EDADESASKP KFGSRQAKAI SVSSRRKNNR REVAGKIDEA
AFVDFNYELD EEYPPERCED LERSYWKTLT YAPPLYGADM PGTLFTDETT SWNLGKLDNL
LDVMGSKIPG VNTAYLYLGM WKATFAWHLE DVDLYSINYI HFGAPKQWYS IAQGDARRFE
AAMKTIWPTD AKACDQFLRH KTFLISPAHL LSNFNIKVNK IVAHPGEFVI TFPYGYHSGY
NLGYNCAEAV NFGLEEWLEY GRVAKKCDCD QAQDSVWINV HELERKMRGE ETEYEETDEE
DEEEEDDGFP TPPGSNGDSK PKIIQKKRKR SANDKSGNDK IKRVRIRIKA PSKEPCILCP
NDIPSEDLLP TEEIGSKAHR ICAMYIPETS VDEDNTKEFV TDVKYIDKAR LELKCNYCRS
KKGACFQCSQ KKCTRAYHAT CAAAAGVSVQ QGEVPRFGED GTEYKEWGIE FSCRFHRTKR
DKKFDGDALE SDERLREGGA KLKIGEVCQA QYYRGDIFAG AVVENRRSEE TVLLDILPRG
DRLEVEYKWL LIPDPADYHL DKPSANAIPM PKSRKDKQSL NTSKRQADDN PRRDDPFVEG
CTWAEFKMEE IARNVAQRKV DLAKEGGLWH YLGRNSTEAR AQFTEDPAKP RNNPKANFLD
TLPRAVPQAL PRHSYSASYP TKTSHPSPNV PRAPSRPLPP SSIKSDKPYA YKPRDIGDTY
RVDQQAYRSQ QSFLQQSAPS VPYSFGTDPR YQTTDPNRPS QYSRPASGSP LAPPPVGPLA
PPTQYRPPYP APIPPRPNNP FTNRAPQNSR PSKPNPFANY TYLQKEHNRS PLEYKSPYRP
GGGFMNGYQG NLGQHLQQTL FQKQSGSTAQ NSTLYTSPRA PYIAGQPSPT VGSYAPSNAA
PHANYGGTTA SSQKQPPAPG GMPTVAPNSW DRRDSPQLHA AIRQEYTQSP MFHQHYQPQH
QPTQYQGSAV LQPPPMWNRQ AYQPGQMPQP NQGPPQQNQG NNPASYSQAQ RQQQPQVTQA
QSYHTSPGPQ TANGSWQSRQ FSQAAPSHQP PQYQSSNPGT QSSPLNSMYA PSQPQGQYRP
SSSYQSAQPL SSIAQKAIHS PINHGQSSPT LQDQENKAVY PHQQYFQKQA QVPQPYARAP
QTYEPADVPV DSTSIIEKIM LNLKGAKPAN A
//
