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Database: UniProt
Entry: A0A0S7DY73_9EURO
LinkDB: A0A0S7DY73_9EURO
Original site: A0A0S7DY73_9EURO 
ID   A0A0S7DY73_9EURO        Unreviewed;      1081 AA.
AC   A0A0S7DY73;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GIM40256.1};
GN   ORFNames=ALT_008743 {ECO:0000313|EMBL:GIM40256.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM40256.1};
RN   [1] {ECO:0000313|EMBL:GIM40256.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM40256.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005995}.
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:GIM40256.1}.
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DR   EMBL; BCLY01000009; GIM40256.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7DY73; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_5851; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   PANTHER; PTHR10742:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   3: Inferred from homology;
SQ   SEQUENCE   1081 AA;  118890 MW;  2CA1305EFB9143F4 CRC64;
     METTASMGLQ GLNGLSYDLS QFDHYLSQAT SYVNGNQHLQ YPSLLNETIP GTGDQSEPPA
     KRLRRSPSCN ELNQSNGETS SPAAIIDPST RPQDGNGVLD RVAGGSESTD SVTHDLNEDT
     SNILSGSATS VSLIYEPSQK DSTPPSTVNN VPFSSSISSD FKGLSGSADY ARYRPRSSIP
     SKLTAAVYAQ QCVTAAYACR LNPYSLHKKE QEALQDHLCH LHVTAYLNIR NGILRLWTRN
     PMVSVTKDEA LGCAKDYRWM GLASFAYEWL VRNGYINFGC VEIPPALVAP RKGRRKDGPV
     IVVIGAGMAG LGCARQLEGL FKQYHDTLTS PRVVVLEGRR RIGGRIYSHP LRSLQSSKLA
     PGFLPKAEMG AQIIVGFEHG NPLDQIIRGQ LALPYHLLRD ISTIYDIDGS AVDEVQDAMD
     ERLYIDVLDR SGLYRHNAVI VPTAEGDRGL IDSGRDLTMS DGLTVRQYEE ARAAGTVELL
     FPNKKVRRGV GHKTADIKAT VPPAPTDLGP TEEQPAALAC QAMGWKLRDG VSATASLNLD
     PVAKASGSPT LGAVMDEGVK QYQRMLPLTP KDMRLINWHF ANLEYANATN IGKLSLSGWD
     QDLGNEFEGE HSQVIGGYQQ VPYGLWSLPT KLDVRTNKIV SKIAYDSTGS GKRKTVVHCE
     DGESFVADKV VFTGSLGVLK HASIEFSPPL PDWKRGAIER LGFGVMNKVI LVFEEPFWDT
     ERDMFGLLRE PKNRDSMVQE DYAANRGRFY LFWNCMKTTG LPVLIALMAG DAAHQAECTP
     DGEIIAEVTS QLRNVFKHVA VPDPLETIIT RWATDRFTRG SYSYVAAQAL PGDYDLMAKP
     IGNLHFAGEA TCGTHPATVH GAYLSGLRAA SEIIESVLGP IEIPNPLVPE KGKTIELGTP
     VATAQKKKEA HFSNGFSAPV STSADPTDAS APARSNNSFS GDTALRQAYE QAMWTAIHAE
     LGPPEPRPAR TGLNPFLLYQ KDYWGKARAQ CDEAKQATTK DPNAKAARDE IRQALGLMWR
     QASEEEKRPY IEQTEVNRQT NTEIWDRWKQ NTKEWERKSL EVKERWCAAN PFESWRPPAK
     R
//
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