ID A0A8J2I216_9PLEO Unreviewed; 1354 AA.
AC A0A8J2I216;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
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=ALTATR162_LOCUS3490 {ECO:0000313|EMBL:CAG5154161.1};
OS Alternaria atra.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Ulocladioides.
OX NCBI_TaxID=119953 {ECO:0000313|EMBL:CAG5154161.1, ECO:0000313|Proteomes:UP000676310};
RN [1] {ECO:0000313|EMBL:CAG5154161.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CS162 {ECO:0000313|EMBL:CAG5154161.1};
RA Stam R.;
RL Submitted (MAY-2021) 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:CAG5154161.1}.
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DR EMBL; CAJRGZ010000016; CAG5154161.1; -; Genomic_DNA.
DR RefSeq; XP_043167033.1; XM_043311098.1.
DR GeneID; 67015052; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000676310; 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:UP000676310};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 69..110
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 340..503
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 597..720
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..59
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..212
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..226
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 555..570
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1027
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1205
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1280
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1314
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1354 AA; 151963 MW; E0510730CB1198D8 CRC64;
MEALPDVVPS VEAPLSTPDD STTKPALTPP TSEDNDKRFE RMSSELSELD DSDDGEDIEP
DHYFEGGKIP VFKPTMDQFR NFKRFIDKID KHGMKSGIVK VIPPAEWRES LPDLTEAVKS
IKVKNPITQE FAGQHGIYTQ ANIEKQRSYN LPEWRAVTDE PHHQPPAKRG ERRKAAAEAP
SRTRSSRAAP ANRDALPAPK RGPGRPSRKR QVKKEPVDDE DEDDSSLEVP PTPTSPGKEE
KKAPARRVKK EARDTTPARA RGRQTKTADE KKSVSSRRLN NRGAVADYID EAAFEDFDYH
LPGLEEYTVE RCKELEDNYW KTINYGSPMY GADMPGSLFD DSTTSWNVAK LPNLLDVLGT
KVPGVNTAYL YLGMWKATFA WHLEDVDLYS INYIHFGAPK QWYSISQEDA RRFEAAMKTI
WPNDAKHCSQ FLRHKTYLIS PQRLERDFDI KVNRLVHYEG EFVITYPYGY HSGYNIGYNC
AESVNFANES WLSYGRIAKK CMCESDSVWV DVNEIERKLR GEPTPEYYEE TDDEDDDDDG
VDRLPSPPAS VAGKTKGRPG RKPAGNKRKR GKEDPKETSR PKKLKRIRIR IRIPGRGMPC
ILCPNDVEYD DLLPTDTGMQ AHRICADYTP ETYIVNKGDV ETVCNVANIG KDRLELKCNY
CRSKRGAVFQ CSQKKCTRAF HATCAVAAGV QVDLGPMPTF DEEGTEYFYD GYDFRCRFHR
PKKRNNKTVD VEALEKDKFV LAYGKTLKPK DVIQFQYVGG EMYQIYGAQV VENRPGEQAV
LVDVLPDGDR VEVEWKYILK LHPDESQRLK PSANAKPLPE HLKESDASLD ITNRTDGVPE
MGDPFHDPNS EHKWAEWYTA PEVTQRVARV DLGKEDRLWY YLGKPSTEAR PQYTENPAKP
RNNPKSNFLD TVKPPPPPVP AFHRTSYPAS YPIKPAPIVV PPRTPMQHQV SDGRPYAYKP
KESMVGSFRS PVYNPDTRKN PNSPVAHQPN VSYDHRMPQG QYGQQSYQGY HSHRPPQSSQ
QQAQYQPYVP PPNYSNASWK AQPATSGPLL NGIDKYAQPP YPYSQSPGRL PPSPYSPVVG
QNAIPSYGPP SRQTQASPHG RSSISKLPSN PTGTPKPPMY AVTPSSNIIY AAQSPTEYLN
YVMNFPYLRN CYLRRTKTYI SPYSLDGGIA PEWMPKPPTP RASGTPTSIA PRPIAPHGAA
PSPGYYGPPP TGLPAPRPSA QFQSPDAFQR EITRTTQAPE APKWEQMLKQ LATSAGPTAT
PSMATHSPQA PQPRYPPPGP RSGTSYDIPR SMQASPNQTP PLPPSREPQR PTPSPISDDG
KSGLVAVPKE QKPVLPPLEP ASNVHGAETW RYSS
//
