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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