ID A0A6A5RI19_9PLEO Unreviewed; 1345 AA.
AC A0A6A5RI19;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 17.
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=M421DRAFT_102167 {ECO:0000313|EMBL:KAF1926738.1};
OS Didymella exigua CBS 183.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Didymella.
OX NCBI_TaxID=1150837 {ECO:0000313|EMBL:KAF1926738.1, ECO:0000313|Proteomes:UP000800082};
RN [1] {ECO:0000313|EMBL:KAF1926738.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 183.55 {ECO:0000313|EMBL:KAF1926738.1};
RA Haridas S., Albert R., Binder M., Bloem J., Labutti K., Salamov A.,
RA Andreopoulos B., Baker S., Barry K., Bills G., Bluhm B., Cannon C.,
RA Castanera R., Culley D., Daum C., Ezra D., Gonzalez J., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B., Goodwin S., Spatafora J., Crous P.,
RA Grigoriev I.;
RT "101 Dothideomycetes genomes: a test case for predicting lifestyles and
RT emergence of pathogens.";
RL Stud. Mycol. 0:0-0(2020).
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; ML978975; KAF1926738.1; -; Genomic_DNA.
DR RefSeq; XP_033446990.1; XM_033586736.1.
DR GeneID; 54344382; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000800082; 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:UP000800082};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 70..111
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 343..506
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 600..719
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..543
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..573
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1345 AA; 150558 MW; 0C36B50C31D9D301 CRC64;
MDTPADVVQS VETPPAVQLH DAIPKAALTP PTSEDNDPKR AERASSELSD VDSDDGEDIE
PDHYWDEGKI PVFKPTMAQF HNFKRFIDKV DKHGMKSGIV KVIPPAEWRD SLPDLHEAIK
SIRVKNPITQ EFTGQHGVYT GANVEKQRSY NLPEWRAVTD EPHHQPPAKR GETRAGRKAE
PPTRTRSTRA APKTDDGTPA PKRKPGRPAR GRRSVKKEEV EDEDDDEAEN LDVPPTPTSP
GAEDVKPARR GGRVKKEDTP TRPRGRQPRA NNEKMSVSSR RLNNRGAVND YIDEAAFEDF
DYHLEGLEDF TPERCKELEE SYWKTIWSGQ PMYGADMPGS LFDDRTTSWN VAKLPNLLDV
LGTKVPGVNT AYLYLGMWKA SFAWHLEDVD LYSINYIHFG APKQWYSISQ EDARRFEAAM
KSIWPNDAKN CSQFLRHKTY LISPQRLEKD FNIKVNRLVH HEGEFVITYP YGYHSGYNIG
YNCAESVNFA TESWLSYGRI AKKCDCESDS VWVDVDEIER KLRGEPTPEY YEETDDEEDE
EDGADRLPSP PASVAGGRTK KKPGRKPAAK RKRGKDEPQE AARPQKLRKI RIRLKIPGRG
MPCILCPNDV DYDDLLPTDN GLKAHRICAD YTPETYIQNE TVCNVANIGK DRLELKCNYC
RSKRGAVFQC SQKRCTRAFH ATCAVAAGVQ VDLGIMQTFD AEGTEYYYDG YDFRCRFHRP
KKRNNKTVDV DALEKNKWIL NYGKTLKPKD VIQFQYVGGE MYQIYGAQVV ENRPGEQSVL
VDVLPDGDRV EVEWKYILKL HPDETQRPRP SENAQSLPEH LKENDASLGM ANRTDGVPEL
GDPFHDPNSE HKWAEWSTAP GVKHRVKKVD FNKENRLWYY LGKPSTEAKP QYTEDPTKPR
NNPRSNFLDT VKPPPPPIPT FQRQSYPASY PIQPAPPGMA RIPYQQQVAP AGGRPYTYKP
KDGMMTTWKS PAYNPDTRQN PNSPVAHQPN VTYDYRASPQ YNYPPPRPLP QQHQYQPYAP
PPHNYSAQGY ASKAASSGPL LDGLDKYAHT NQSHQALPPY SYQTQSSAQA PRQLPYPDSS
TAPYGSPAQH GQAPPSHGRA SIPNMLSTPT GTPKPPMYAV TPSSSVVPAA QNSTEYLAYV
MKYPYLKNAY LRRQKTYISP YSPGGGIAPE WMPKPPQIAS GATPTSMRNG STGSHGYYPS
PSPSSIAPRP SAQFQSPDAF QRGLTQTSSS STGAPKWEQM LKQLATSTGP IATPSALTSQ
TSQTPQYPPL PRSSTSYGML NAPGPFQKHT SPLPQPGEPQ RPIPSPISDD GKGGVVATKS
VLPPPPAIQA VPGQMHSAET WRFSQ
//
