ID I8I6T1_ASPO3 Unreviewed; 1395 AA.
AC I8I6T1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=Ao3042_01293 {ECO:0000313|EMBL:EIT72461.1};
OS Aspergillus oryzae (strain 3.042) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1160506 {ECO:0000313|EMBL:EIT72461.1, ECO:0000313|Proteomes:UP000002812};
RN [1] {ECO:0000313|EMBL:EIT72461.1, ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|EMBL:EIT72461.1,
RC ECO:0000313|Proteomes:UP000002812};
RX PubMed=22933657; DOI=10.1128/EC.00160-12;
RA Zhao G., Yao Y., Qi W., Wang C., Hou L., Zeng B., Cao X.;
RT "Draft genome sequence of Aspergillus oryzae strain 3.042.";
RL Eukaryot. Cell 11:1178-1178(2012).
RN [2] {ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|Proteomes:UP000002812};
RA Zhao G., Hou L., Wang C., Cao X.;
RT "Comparative genomic analyses of Aspergillus oryzae 3.042 and A. oryzae
RT RIB40 for soy-sauce fermentation.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; 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:ARBA00000040};
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:EIT72461.1}.
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DR EMBL; AKHY01000216; EIT72461.1; -; Genomic_DNA.
DR HOGENOM; CLU_001442_1_3_1; -.
DR Proteomes; UP000002812; Unassembled WGS sequence.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 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; 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; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 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 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 18..53
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..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1395 AA; 156225 MW; 4A5798333CCEFA61 CRC64;
MMATALDQPL FESVAGPATA AASITPPHSA NGKKEVPDGV PSELSDLELD PNAVGVPEAA
SVEEEEEDIE PDHYYGGGKI PVFKPTMDQF RDFQSFINKV EKYGMRSGIL KVIPPKEWTD
SLPALDEAVK KIRVKNPIMQ EFHGSHGTYT QANIERQRSY NLPQWKGLCE ESSHQPPARR
GERRRNQERI TRAPPSSRAQ TARPDSQKRR PGPGRPPKRS NQVKVKEEPA EDTIDKIKPE
GPPTPVSPES NPVEAKTEEL SDGESLPAPK PKGRQPKSVT SRRKHNKGDA IDYVDEEAFK
DFDYRIHDNE EYTQERCEEL ETAYWKSLMF NNPLYGADMP GSLFDENITT SWNVARLPNL
LDVLGQKVPG VNTAYLYLGM WKATFAWHLE DVDLYSINYI HFGAPKQWYS ISQEDAPKFE
QAMKSIWPSD AKNCDQFLRH KTYLVSPSLL KSQYGITVNR LVHYEGEFVI TYPYGYHSGY
NLGYNCAESV NFATEKWLDY GRVAKKCHCE SDSVWIDVDE IERKLRGEAT PEYYPEFESD
LDEFEGASDL LTPPRSVPEK SNRGRKRKHD GDTTKAKRMR VNVHVPRKIP CVLCPNDLDY
EDLLPTEDGK NHAHRRCALY TEETSILRDE TGKEVVCDID KIPKARMGLK CLFCREVRGA
CFQCNFGKCT RSYHATCALL AGVQVEQGEI AVIADDGIHY SIPSVDLKCK YHRQKKPSWM
TGGDSPDFDR KLIESAQRMV AGDLVQFQAD KEINGAVVLE NRPAERTLLV KVLPRGDVIE
LPYRWMLVVR RSNFSPLAPG TKPLPAHLAR KPEARKELES ALPVVGNPFG DGRSPYQWAE
FETVDTTNHR FAPPPVQVKL DKGDQIWYYL GQSSTECRAQ YTHNPSVPVH NPRSNFLDSV
KSLGAVMARI PSYPHRHLPQ YATAPPHHLS PAAAAAATAA AAASRPSLLQ RPTLAPPPRT
PSSAAPPAST AMPSAYRSLP TQSARHAPYP QIAKTHQSHH LSQQQHSPQQ SQQQQQQQHS
HHLPANTFAN VRELIARRRL AQITDHANVF AGYTIVSPEL VVETLLGPMG SVPPPTGLEK
LELAMAQQRV QPRAADGTLL PLQPLNMRSE EVTRLLQMLR FSLVSHRDRL DVLQKKETEN
NKQESAHKGS VAAVKLPRKF AYLEQQQEQS PTVYQSPYNM PSGFSEYAQK TFGLTPSEPE
LPKPSLANDY FASLSPEDQE KILKTCGSFV QRAIERSASH SRQSSASNLR LASALAQQTE
NPTIDITTVE DMPLSGLDFP LHADSPCSSF SRPHLRFQSP NDYNAHGPET HHDHHDLFGD
QQANTRFWQH GPWAAGDGNT PNEETRPFFG PHERLKHDYA SSDISLGRGP GSLHSVDMAG
FGMDATDDLC NVLSP
//
