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Database: UniProt
Entry: A0A395SBB5_FUSSP
LinkDB: A0A395SBB5_FUSSP
Original site: A0A395SBB5_FUSSP 
ID   A0A395SBB5_FUSSP        Unreviewed;       735 AA.
AC   A0A395SBB5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=L-amino-acid oxidase {ECO:0000313|EMBL:RGP69694.1};
GN   ORFNames=FSPOR_4506 {ECO:0000313|EMBL:RGP69694.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP69694.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP69694.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP69694.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP69694.1}.
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DR   EMBL; PXOF01000059; RGP69694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395SBB5; -.
DR   STRING; 5514.A0A395SBB5; -.
DR   Proteomes; UP000266152; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.20.1440.240; -; 1.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR10742:SF342; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT   DOMAIN          154..636
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   REGION          670..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..704
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   735 AA;  81240 MW;  92F643F083EE4638 CRC64;
     MKHSIASLAL SVGSSFASSL PVQLETREPL TSHLANIHVR FSKPTEDALS FTYGPCDAKS
     ISEAHHTIAT TDSKSVSRLA WVIPANTNDN GCISAWTNDG ALVGRNSVHM TEENGFDVLG
     PWFDGVAHLT KTGTSFVDEE AAKAKEIAIV GAGMSGLMTY LVLSQAGMTN VSIIEAGQRL
     GGRVHTEYLT GGPFDYSYQE MGPMRFPSTY TSPETNETMN ITDHQLVFQL AEEMNNLNNH
     DKNLSVDFIP WIQANSNGLS YKNEFKLPNG MPPTLAQISK NASLGAASDL GPEAKDLQAK
     LDTFMPGSDF STLMAKNMFK AHKQWLETGL NGLGGDQWSE YAFMVNYLKG SLNSTDVLGD
     WSAATFWDTL YEGLYFSAAS YKTIDGGLNR LPLSFHPLVD DITTMGRKIE RVRYNDTDDK
     VTLQWRKEYN DTEFQDSTFD YAVIAVPFSI VRRWRLPNLP ATISNAIKEL NYGSACKVAL
     EFSERFWEHY ENPIIGGCST TSDIPGIGSI CYPSYNINGT GPATILASYI SGDMGYRLAS
     MSEEDHVQMV FDAMVDIHGE FIRELYTGKF NRRCWALDPL QSGSWASPTA GQHQLYIPEY
     FKTYDKMIFV GEHTSYTHAW IASALDSGIR GAVQLLLELG LIDEAKQAVD KWMARWIEVD
     EDLDIVAERA WTEEETDIEN TDTEDDMNAD DYVAFSDEED HEDSNEAGGS TRSSNGSVGH
     LDFAAAEAEE DNASV
//
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