ID A0A5N6Z3W7_9EURO Unreviewed; 1402 AA.
AC A0A5N6Z3W7;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 28-JAN-2026, entry version 19.
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=BDV28DRAFT_4033 {ECO:0000313|EMBL:KAE8352345.1};
OS Aspergillus coremiiformis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=138285 {ECO:0000313|EMBL:KAE8352345.1, ECO:0000313|Proteomes:UP000327118};
RN [1] {ECO:0000313|Proteomes:UP000327118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 553.77 {ECO:0000313|Proteomes:UP000327118};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics studyof 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) 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; ML739134; KAE8352345.1; -; Genomic_DNA.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000327118; 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:UP000327118};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 80..121
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 346..509
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 586..711
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..218
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1016
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1402 AA; 157133 MW; 61531C66B3854767 CRC64;
MMATALDQPP FESAAGPATT AASITPPHSA NGKKEVPDGV PSELSDLELD LNAAGAPEVA
SVEAEEEELE PDHYYGGGKI PVFKPTMDQF RDFQSFVNKI EKYGMQSGIL KVIPPKEWTE
SLPPLDEAIK KIRVKNPIMQ EFHGSHGTYT QANIERQRTY NLPQWKGLSE ESSHQPPARR
GERRRNQERV TRIAPSSRTQ PTRSDSQKRR PGPGRPPKRS NQVKVKEEPS EDSLEKIKPE
DPPTPVSPES NPVETKTEEL SDGESLPAPK PKGRQPKSVT SRRKHNKGDA IDYVDEEAFK
DFDYRIHDHE EYTQERCEEL ETAYWKSLMF NNPMYGADMP GSLFDENITT SWNVAKLPNL
LDVLGQKVPG VNTAYLYLGM WKATFAWHLE DVDLYSINYI HFGAPKQWYS ISQADAPRFE
QAMKSIWPSD AKNCDQFLRH KTYLVSPSLL KSQYGITVNK LVHYEGEFVI TYPYGYHSGY
NLGYNCAESV NFATEKWLEY GRVAKKCHCE ADSVWIDVDE LERKRRGEST PEYDREFESD
LDEMEGASDL LTPPRSVPEK SNRGRKRKHD GDLTKAKRIR VSVERKIPCV LCPNNLDYED
LLPTEDGKNH AHRRCALYTE ETSILRDETG KEVVCDIDKI PKARMGLKCL FCREVRGACF
QCNFGKCTRS YHATCALLAG VQAEQGAIAV IADDGNQYSI PNVDLKCKYH RQKKPSWMSS
GDSPDYDRKL IGTAQRMVAG DLIQFQADKE INGAIVLQNR PAERTLLVKV LPRGDVIELP
YRWMLVVRRS NFSPLTPGTK PLPAHLARKP EGRKELESAL PVVGNPFGDG RSPYQWAEFE
TVDTTNHRFA PPPVQVNLNK GDQMWYYLGQ SSTECRAQYT HNPSVSVHNP RSNFLDSVKS
LGAVMARLPS YPHRHLPQYV ASPLHHLSPA AAAAATAAAA AASRPSLLQR PPLAPPPRTP
SSPASVVTAM PSAYRSLPTQ SARHAPYPQI AKTHQSHHLS QQQHSSPPPP PPPPPQQQQQ
QQQQQHSHHL PANTFANVRE LIARRRLAQI TDHANVFAGY TIVSPELVVE TLLGPMGSVP
PPSGLEKLEL AMAQQRVQPR APDGTLLPLQ PLNMRSEEVT RLLQMLRFSL VSHRDRLDVL
HKKETENNKQ EPVHRAGVAA AKLPRKYAYL EQQREQTPSV YQSPYDMPFG FTDYAQKTFG
LTPCEPELPK PSLANDYFAS LSPEDQEKIL KTCGSFVQRA IERSTSHSRQ SSASNLRLAS
ALAQQTENPT IDITTVEDMP LSALDFPLHA DSPCSSFSRS HLRFQSPNEF TSHGAEVHHD
HHDLFGDQQA NTRFWQHGPW AAGDGNTPNE ETRPFFGPHE RLKHDYASSD ISLGRGPGSL
HSVDMAGFGM DATDDICAVL SP
//
