ID A0A319BTE0_9EURO Unreviewed; 1059 AA.
AC A0A319BTE0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Flavin-containing amine oxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO82DRAFT_387747 {ECO:0000313|EMBL:PYH75824.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH75824.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH75824.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH75824.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; KZ821776; PYH75824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319BTE0; -.
DR STRING; 1448315.A0A319BTE0; -.
DR VEuPathDB; FungiDB:BO82DRAFT_387747; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000248340; Unassembled WGS sequence.
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 CDD; cd00084; HMG-box_SF; 1.
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; 2.
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;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000248340}.
FT DOMAIN 120..215
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 908..988
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 908..988
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 819..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1059 AA; 116631 MW; BA29122B0B66CBC8 CRC64;
MASSGGQFSM FSARHIFPES SQPARLPAMI QPTRVYATGL VNPNGAMAST ATPTLNGSAM
QPSALESTNP SQRLNGQFAV AATTPTASIA STLHASNGTT YRPRSSIPPR MPAAVYAQQC
VEAAYASRLN PYALHKNEQD ALQDHLCHLQ VTMYLNIRNG ILRLWTRNPM VSVTKEEALG
CTKDYRWVNL ASFAYEWLIR NGYINFGCVE IPAALVSPRK GRRKDGPVIV VIGAGVAGLS
CARQLEGLFR HYHDADSSPR VVVLEGRRRI GGRIYSHPLR SLQSSKLAPG LVPKAEMGAQ
IIVGFEHGNP LDQIVRGQLA LPYHLLRDIS TIYDVDGSAV DEPRDATAEM LYNDVLDRSG
FYRHKSVIVP TAEGERDLID NGRDIVTNDG LTVRQYEEAR AAGTIGLLFP AKKVRRGVGH
KTAEIKPVGA PSANADRNEE NPTKLACQTM GWSLKHGVSD TEKINLDPIA KASRNQTLGA
VLDEGVRQYQ HMLPLTPKDM RLMNWHMANL EYANAANVGK LSLSGWDQDM GNEFEGEHSQ
VIGGYQQLPF GLWSLPTKLD VRPNKVVCRV SYDQTGRGKQ KALIQCEDGE SFMADKVVFT
GSLGVLKHRS IQFSPPLPEW KLGAIDRLGF GVMNKVILVF DQPFWDTERD MFGLLREPQN
RDSMRQEDYS ANRGRFYLFW NCMRTTGLPV LIALMAGDAA HQAECTPDAE IIAEVTSQLR
NVFKHVAVPD PLETIVTRWA SDKFTRGSYS FVAAHSLPGD YDLMAQSIGN LHFAGEATCG
THPATVHGAY LSGLRAASEI IDHTLGHIEI PTPLVPEKGA KVVPPGDILH APSTTTPTTA
TTGQKRKQQH HPSSAATTSS IHPLLSNPQP IDPNDPNPSP ESLRRAAYDK AMWAAITAEI
GAPLPRPARA VLNPFLLYQK DVWTRCRAQC DEARRAATND PTAKAPRDEI RQALGQMWRQ
ADPAEKRPYL ERIEANRQAN AAVMEHWRRE VAEWEKRALQ VRERWCREHP FDGNSSTSIV
NSTSVSSAGN APTSIQAMVP TAQQHQPQPQ QQVNDSTHS
//
