ID   A0A139HGN4_9PEZI        Unreviewed;       434 AA.
AC   A0A139HGN4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01266};
GN   ORFNames=AC578_8016 {ECO:0000313|EMBL:KXT01610.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT01610.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT01610.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT01610.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KXT01610.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LFZN01000052; KXT01610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HGN4; -.
DR   STRING; 321146.A0A139HGN4; -.
DR   OrthoDB; 1952715at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR045170; MTOX.
DR   PANTHER; PTHR10961:SF26; FAD DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT   DOMAIN          8..382
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   434 AA;  48258 MW;  2C9DE25640B9BA34 CRC64;
     MPSKRSPIAI VGGGAWGLST AQHLTKAGYT DITVYERAEK IPSPYSAAWD INKIIRAEYE
     DPFYTNLTLE AIEQWKTPLY GPYFHQTGYV VAATGRAPAK AVKHLEEALS NVENHPAFKS
     GIRRLESAKD FKDYTWQYSG PLNGWKGYYN RLAGYGHSAD ALKGIWEHCA RIGVKFVLGE
     SAGKVDKLLY SGSKCVGLET ADGKKHKADL TICALGAHGA DLLPGLGKFV TARAWSVAHV
     QLNEDEANFL RGIPTTNVRD LGFFFEPDPK TKLFKLCPLG VGFTNTGSDG VSLAPKERLP
     QPQDFIPAED EQKLRQLLRE TFPWMADRPF VDQKLCWFAD TADSDYCIDF VPGTQNSVVA
     LSGDSGHGFK MMPIVGKWVA QLLGDGKQSE QRWMWKSVDL TKQNWGEKVS WRIGKGAELR
     DLLKAKEKLI RARL
//