ID A0A8E5HUL6_USTVR Unreviewed; 1371 AA.
AC A0A8E5HUL6;
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};
GN ORFNames=UV8b_06130 {ECO:0000313|EMBL:QUC21889.1};
OS Ustilaginoidea virens (Rice false smut fungus) (Villosiclava virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Ustilaginoidea.
OX NCBI_TaxID=1159556 {ECO:0000313|EMBL:QUC21889.1, ECO:0000313|Proteomes:UP000027002};
RN [1] {ECO:0000313|EMBL:QUC21889.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UV-8b {ECO:0000313|EMBL:QUC21889.1};
RA Zhang K., Zhao Z., Zhang Z., Li Y., Hsiang T., Sun W.;
RT "A mixture of massive structural variations and highly conserved coding
RT sequences in Ustilaginoidea virens genome.";
RL Submitted (MAR-2020) 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}.
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DR EMBL; CP072757; QUC21889.1; -; Genomic_DNA.
DR RefSeq; XP_042999562.1; XM_043143627.1.
DR GeneID; 66066907; -.
DR KEGG; uvi:66066907; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000027002; Chromosome 5.
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:UP000027002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 138..179
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 415..578
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 665..785
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..91
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..117
FT /note="Low complexity"
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 267..281
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..328
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..619
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1275
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1371 AA; 152345 MW; D0661F3609A39BF2 CRC64;
MSTDVVSASE PRGPPVTAAP GPSRDSPPDA PSIGPHPIPD TAKLPAHGQD EIECAKPAAP
IFLHSPPDSN NATKSDASDS ELSELEEEPT LDDAPSATAF TTAPAPTSAP ALEPAPSKLI
GDEEDIGEVL PEEWSGAVPI FRPTWDQFKD FKKFMNKVDC YGMKSGIIKI IPPREWKDAQ
PPLDELVKQI RVREPIKQDI MGSNGTYRQV NILHGRSYNV PQWRQLCEQS EHQPPARRGE
RRANADKYKQ VRPRPSNASK TNTPTTPKRR GRGRPSKNKG KKTIDENEER PMTPVSPGPE
MEAGAEDKPV ESIEQEVGDE TKETDDESTV GRTGGRMGAV KPSKPKTQSV SARRKYSRRE
GSAMIDEAAF RGFDYRLDVS EFTPERCEEL ERAYWKTLTY AAPLYGADMM GTLFDDRTEN
WNLNKLPNLL DVLGTKIPGV NTAYLYLGMW KATFAWHLED VDLYSINYLH FGAPKQWYSI
SQADARRFEA AMKSVWPADA KACSQFLRHK GFLISPQYLL QHYGIRVNKV VSYPGEFVVT
YPYGYHSGYN LGYNCAEAVN FALDTWLEMG KIAKRCECAQ AQDSVWINVH EIERKLRGEE
TEYEETEDED DEDEDDEEQS SLPTPPASSS VKLKDASRKR RRGVDEKGAK TRVKKLKLRL
KTKAEPPCCL CPNDVSIFEL LPTEDGRKAH KLCALYLPET YIDVVEGQEI ICNAGGVHKD
RLNLKCLFCR SRRGACFQCS HKKCARGYHA TCAAAAGVFV EDQHVPVFDE NGIEYKEQVF
EFNCRFHRVR RDKRVEGESL ETDGTIRNAA QKLKVGDICQ MQYLKGDIFA GIVVENREVD
ETLLLEILPN GDRLEVAWKW LLLPDPLDYR LPKASDNALP MPATRKAKDQ LNATRPHEDR
PRKDDVFAEG YTWAEFEVHE VHNKDQCKVS FEKPDQMWHY LGKTSTEAKA QYTENPDLQR
HNPRGNFLNT VPKPSKPPKP PKPCKPAKPP KPALVSQPGY NHASYVAKAM AYSYNLAANH
AANHAANYAA ATTTPRPVTF DKPHVYTPRQ TANNKLTTPS TPAAFATHPS VSNSSPPVGP
APVFYNYSHP SSAFAKQSPC HHQNTLSNGR SQLGQPLAAA PVHSVPCKPV LAPSTQPGKP
LWQVHSSIYQ KYPFFQVNHN RDPSRYRTPY SPHGGFLNGY EGDLRAHLMA NQNELTRPFS
TWGLSSWSAA PGITQQALPF QATKPRPAPI VKKFKIPSKV SPVPLPPHVV AAMTKASPPA
SGSESTSGET GATSPRSTAA PVISPQAANG PDAARTSDAT ARSFNATWQG GPAQDKVDLG
ITSAETMFTM ERPKATQEFA DVPGSESMQF VERMMQNLKK VSMNDTERKD G
//
