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Database: UniProt
Entry: A0A139HW43_9PEZI
LinkDB: A0A139HW43_9PEZI
Original site: A0A139HW43_9PEZI 
ID   A0A139HW43_9PEZI        Unreviewed;       438 AA.
AC   A0A139HW43;
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_8566 {ECO:0000313|EMBL:KXT06609.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT06609.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT06609.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT06609.1,
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:KXT06609.1}.
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DR   EMBL; LFZN01000005; KXT06609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HW43; -.
DR   STRING; 321146.A0A139HW43; -.
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:SF45; L-PIPECOLATE OXIDASE; 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..393
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   438 AA;  48856 MW;  D541287A4B2445AF CRC64;
     MASNTKSYVI VGAGVFGVST AYHLKKQYPN AEITIVDRDA YDADSRVAAS WDWNKVVRAD
     YDDIVYCQLA LESQDVFKSD PLWKPYFHET GIYWVCRDDY AGKVIDNYKK LGRKAELQSV
     SIEDAKKMHN GLFDLADYDR AKSVLVNKTS GWAAAGDCLR AVTKWCLEQG IKYEVAEVAS
     LQFSGDRCTG VRTTSGKTIS GDHVILSSGA YTPKLLELAA QASGNIELRA GRRITAGGIT
     TGMTTLKGRD IETFADMPVG VQGYTAATGP FIGSLPPTKD NELKWWGQTI FENTQELFPG
     RWVSYPPSKP DYGQWDASRR MREDIDHANQ VFYGKKGANW KMEKYRVCWD AFTTDADFII
     SPHSAANGLY VATCGNFHGW KFFPVIGKYV VQMLDGKLSP ELSQKWAWDR ARPDPSGNAD
     YPRAQLSTLL DPVRTSKL
//
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