ID A0A5N7A8V7_9EURO Unreviewed; 1400 AA.
AC A0A5N7A8V7;
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=BDV27DRAFT_144804 {ECO:0000313|EMBL:KAE8365010.1};
OS Aspergillus caelatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=61420 {ECO:0000313|EMBL:KAE8365010.1, ECO:0000313|Proteomes:UP000326268};
RN [1] {ECO:0000313|EMBL:KAE8365010.1, ECO:0000313|Proteomes:UP000326268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 763.97 {ECO:0000313|EMBL:KAE8365010.1,
RC ECO:0000313|Proteomes:UP000326268};
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; ML737639; KAE8365010.1; -; Genomic_DNA.
DR RefSeq; XP_031928091.1; XM_032070307.1.
DR GeneID; 43654753; -.
DR OrthoDB; 9547406at2759; -.
DR Proteomes; UP000326268; 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; 2.60.120.650:FF:000047; 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:UP000326268};
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 588..713
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 17..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..204
FT /note="Low complexity"
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..239
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 934..953
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..975
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1023
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1400 AA; 156968 MW; B9F712E59819BC6C CRC64;
MMATALDQPL FESVAGPATT AASITPPHSA NGKKEVPDGV PSELSDLELD PNTAGVPEAV
SVEEEEEDIE PDHYYGGGKI PVFKPTMDQF RDFQSFINKV EKYGMRSGII KVIPPKEWTD
SLPALDEAVK KIRVKNPIMQ EFHGSHGTYT QANIERQRSY NLPQWKGLCE ESSHQPPARR
GERRRNQERV TRTAPSSRTQ TTRSDSQKRR PGPGRPPKRS NQVKVKEEPA EDTLDKIKPE
GPPTPVSPES NPVEAKTEEL SDGESLPAPK PKGRQPKSVT SRRKHNKGDA IDYVDEEAFR
DFDYRIHDNE EYTQERCEEL ETAYWKSLMF NNPMYGADMP GSLFDENITT SWNVAKLPNL
LDVLGQKVPG VNTAYLYLGM WKATFAWHLE DVDLYSINYI HFGAPKQWYS ISQEDAPRFE
QAMKSIWPSD AKNCDQFLRH KTYLVSPSLL KSQYGITVNR LVHYEGEFVI TYPYGYHSGY
NLGYNCAESV NFATEKWLDY GRVAKKCHCE SDSVWIDVDE IERKLRGEST PEYDGEFESD
LDEFEGASDL LTPPRSVPEK SNRGRKRKHD GDSTKSKRMR VNVDVPRKIP CVLCPNNLDY
EDLLPTEDGK NHAHRRCALY TEETSILRDE TGKEVVCDID KIPKARMGLK CLFCREVRGA
CFQCNFGKCT RSYHATCALL AGVQVEQGEI AVIADDGNHY SIPSVDLKCK YHRQKKPSWM
TSGDSPDFDR KLIETAQRMV AGDLVQFQAD KEINGAVVLE NRPAERTLLV KVLPRGDVIE
LPYRWMLVVR RSNFSPLAPG TKPLPAHLAR KPEGRKELES ALPVVGNPFG DGRSPYQWAE
FETVDTTNHR FAPPLVQVNL DKGDQIWYYL GQSSTECRAQ YTHNPSVPVH NPRSNFLDSV
KSLGAVMARL PSYPHRHLAQ YAAAPPHHLS PAAAAATAAA AASRPSLLQR PSTLAPPPRT
PSSAAPSAST AMPSAYRSLP TQSARHAPYP QIAKTHHQSH HLSQQQRSPQ QQQKEQQQQQ
QQQHSHHLPA NTFANVRELI ARRRLAQITD HANVFAGYTI VSPELVVETL LGPMGSVPPP
SGLEKLELAM AQQRVQPRAP DGTLLPLQPL NMRSEEVTRL LQMLRFSLVS HRDRLDVLQK
KETENNKQES AQKGGAAAVK LPRKFAYLEQ QREQSPTVYQ SPYDMPSGFT EYAQKTFGLT
PCEPELPKSS LANDFFASLS PEDQEKILKT CGSFVQRAIE RSTSHSRQSS ASNLRLASAL
AQQTENPTID ITTVEDMPLS GLDFPLHADS PCSSFSRTHL RFQSPNDFNA HGPETHHDHH
DLFGDQQANT RFWQHGPWAA GDGNTPNEET RPFFGPHERL KHDYASSDIS LGRGPGSLHS
VDMAGFGMDA TDDLCNVLSP
//
