ID A0A9P8UR43_9PEZI Unreviewed; 1594 AA.
AC A0A9P8UR43;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
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=BKA67DRAFT_655011 {ECO:0000313|EMBL:KAH6656694.1};
OS Truncatella angustata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Amphisphaeriales; Sporocadaceae; Truncatella.
OX NCBI_TaxID=152316 {ECO:0000313|EMBL:KAH6656694.1, ECO:0000313|Proteomes:UP000758603};
RN [1] {ECO:0000313|EMBL:KAH6656694.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MPI-SDFR-AT-0073 {ECO:0000313|EMBL:KAH6656694.1};
RA Mesny F., Miyauchi S., Thiergart T., Pickel B., Atanasova L., Karlsson M.,
RA Huettel B., Barry K.W., Haridas S., Chen C., Bauer D., Andreopoulos W.,
RA Pangilinan J., LaButti K., Riley R., Lipzen A., Clum A., Drula E.,
RA Henrissat B., Kohler A., Grigoriev I.V., Martin F.M., Hacquard S.;
RT "Genetic determinants of endophytism in the Arabidopsis root mycobiome.";
RL Nat. Commun. 0:0-0(2021).
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:KAH6656694.1}.
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DR EMBL; JAGPXC010000002; KAH6656694.1; -; Genomic_DNA.
DR RefSeq; XP_045960928.1; XM_046106665.1.
DR GeneID; 70135556; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000758603; 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:UP000758603};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 129..170
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 398..561
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 648..771
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1535..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..258
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..270
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..605
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1195
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1594 AA; 176988 MW; 021DD8EEA19341D4 CRC64;
MSAEAIAEMA PAPVPVPVLE PVPEPEHAQI EVASATESPN AARASPKPTT GLHSPPDSNN
AMKLDGDDDS ELSDLDDPEP EPPSSHAEPE QSTDVGPDVP AEEHVGVEAA AEQDEDIGPV
LPDHWSGTVP VFKPDMHQFK DFKKFMEKVD PYGMKSGIVK IIPPADWKEK LPDYHDLVKQ
IRVREPIKQD IMGTNGTYRQ VNLLHQRSYN LPQWRQLCDQ SEHQPPAKRG ERRANAERSR
PPPRSKAASS STTTAPKGRS GRATRGRAKK AAIDGASGQD RPMTPVSPKP SEDVMESVEQ
DDPGADVEDE DDAPRAPGRM GASRQPKAKT QSTSARRKYS RREASARIDE EAFKDWDYNM
DISDYTPERC EELERIYWKT LTYAQPLYGA DLLGTLFSED TELWNLNKLP NLLDVLGSKI
PGVNTAYLYL GMWKATFAWH LEDVDLYSIN YLHFGAPKQW YSISQGDARR FETAMKSIWP
TDAKACDQFL RHKAFLISPN HLQSHFNIKV NKVVSYPGEF VVTYPYGYHS GYNLGYNCAE
AVNFALDSWL PMGRIAKKCE CAQAQDSVWI DVHEIERKLR GESTDYEETE DEEDDEEDEE
EDEEESLHTS TVIKIKQPSR KRKRTATDRG EKKAKKIRLR VRIKTQIEPP CCLCPNTILD
SELLPTDDGR KAHRMCALYG PETWVETVDG QEIVANAANI SKARLELKCL YCRSKRGACF
QCSYKKCARS YHATCAAAAG VFVEEGEVPI FGEDGTEYKE QAFEFSCRFH RSKRDKKLNG
ETLDDCKKVL EAAAALKKGD LAQLQYYRGE IFAGVVVDNR HDEQTFLVEI IPNGDRVEVE
WKWLLIPDPS DFRMQKASPN AIPMPTSRTA KERINATKRA VEELPRAQDD FVEGFTWAEF
HTADNPTNKA QVKIDFSKEN QVWYYLGRTS TEARAQYTEN LRKQAHNSKS NFLDTIPRQA
PPVVARQWPA PYNNNPTKVD RPYQYKPKTP VLSAYNPYSY TQQRQPAQPF TPSQHSDQKY
SRQPYTVQQF APNGLATKPF PTSTSTFVPQ GGARPPYNNQ ATPKTVFQSS VPTPQTAPQQ
HYTGLGAVPQ TTPRPVQLPK PTVPHSAPAH SHNKSVPFGT DPRYRTSSTY GSARYDKGSS
SPFSYGIMQP PGLGTTPSPQ NGQVFQAQAR ERSSSAASAM SLPMTSSAIG PSSQGLGSGG
QAQVVKLPIP RPPPPSVLQK YAFFQVHHNR DSTKYRTPYA PWGGFTNGYE GNLRAHLMKT
PDALFGYKKQ SPEMNAALPS IPQYSSETSV GSKSSQNHSP HAAGLEAPQQ SMPLVPSAQG
ASSPATPTPD STKALQTASG SYDPDSVLTK LHPAIRAQYA AMLQRRQSQD QQHTPAPTQS
QPRQEHSSPA PPVTARCPFT PPNAQNLRTS NSVLPLQPAS EHQYQNHVPP VQPQSLPHMS
CSVPQQVPPQ PSADGPQTST IEFQDVLSMV PGHSEQRASP QQRAQPSTPS SQSRPITLRQ
TPVPPPRPWE QLQRAVPATV MPPPPPAQPL ATTTGIDHTM TNTGPETLQP DPNQGHQPSN
VSGPFWQTLP QTMPNSNSLS PQASFDPFQF INFQ
//
