ID A0A6A6ADT3_9PLEO Unreviewed; 1357 AA.
AC A0A6A6ADT3;
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=P153DRAFT_376395 {ECO:0000313|EMBL:KAF2129114.1};
OS Dothidotthia symphoricarpi CBS 119687.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Dothidotthiaceae; Dothidotthia.
OX NCBI_TaxID=1392245 {ECO:0000313|EMBL:KAF2129114.1, ECO:0000313|Proteomes:UP000799771};
RN [1] {ECO:0000313|EMBL:KAF2129114.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 119687 {ECO:0000313|EMBL:KAF2129114.1};
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; ML977507; KAF2129114.1; -; Genomic_DNA.
DR RefSeq; XP_033523503.1; XM_033669653.1.
DR GeneID; 54410085; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000799771; 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 FunFam; 3.30.40.10:FF:000377; 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:UP000799771};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 71..112
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 340..503
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 595..717
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..61
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..540
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..568
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..950
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1027
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1357 AA; 152829 MW; EA3A5B53250102A4 CRC64;
MEALTEVVPS VETASTPTTH HDDVAAKAAL TPPTSEDNDK RDERMSSELS DIDSDDGEDI
EPDHYFEGGK IPVFKPTMDQ FRNFKRFIDK IDKHGMKSGI VKVIPPDDWR NALPDLSEQI
KSIKVKNPIM QEFAGQHGIY TQANIEKQRS YNLPEWRAVT DEPHHQPPAK RGERRKAAAE
APSRTRSTRA QAAPTKTDDA PKRGPGRPRR RQTKTEKKDE DDDADSIDVP PTPTSPGREE
KRTTRRRVKK EDQDDAPPTK ARGRQPKIDQ KKSVSSRRLN NRGAVADYID EEAFDEFDYH
LEGLEEYTVE RCKELEDNYW KTINYGQPMY GADMPGSLFD DRTTSWNVAK LPNLLDVLGT
KVPGVNTAYL YLGMWKATFA WHLEDVDLYS INYIHFGAPK QWYSISQEDA RRFEAAMKSI
WPNDAKHCSQ FLRHKTYLIS PQRLEKDFNI KVNRLVHYEG EFVITYPYGY HSGYNIGYNC
AESVNFANES WLSYGRIAKK CNCESDSVWV DVNEIERKLR GEPTPEYYEE TDDEDDEDGA
DLLPSPPPSV VGKPKKKPGR KPGNKRKRAN DEVQETPRPK KLKRIRIRLK IPGRGMPCIL
CPNDVEYDEL LPTDNGMKAH RICADYTPET WISSKPNEKV CNVANIGKDR LELKCNYCRS
KRGAVFQCSQ KKCTRAFHAT CAVAAGVQVD LGPMPTFDEE GTEYFYDGYD FRCRFHRPKK
RNNKTVDVES LEKDKFVMNY GKTLKPMDVI QFQYVGGEMY QIYGAQVVEN RPGEQSALVD
VLPDGDRVEV EWKYILKLHP EESQRLKPSA NAKPLPEHLK ESDASLDITN RTDGVPEIGD
PFHDPNSEQR WAEWHTAPEV TRRAPKIDFS KENRLWYYLG KPSTEAKPQY TENLALRRNN
PKSNFMDTVR PPPPPVPVFD RRSYPASYPL KPAPIQTQMP PRTPMQQQIR PADRPYTYKP
REGMMTTWKS PVYNSGADTR NNPNSPVAHQ PNVSYDHRAP APPNGQQAYP AYHSHRPPQQ
QQYQYQPYVP PQNNSTSSWK QQPVTAGPLL NGIDQYAHPY QSNQALPPYP YQPPASSQSP
RQLPPFPYAS GSGQNMTPAY SPAGAHNRAT QAPPPSSHGM LSNPSGTPNP PMYAVSPSSS
IVYAATSPIE YLAYVTNYPY LKNAYLRRAK TYISPYSPGG GFTPEWKPKP TTARPAIAPR
PPPAAQQGSH QGHPPAGASA PRPTAQFQSP HDFQREMERA PQAGNGTPKW EQMLKQLATS
TGSATAPTVT APPSYASQSP YPPQPQYTPS SSGPWTQPPQ TESQRPIPSP LSDGATSPQR
PEYSPISDDG NATVAAPSPV PGQSAVHGAG AETWRYT
//
