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Database: UniProt
Entry: A0A0F0IIC8_ASPPU
LinkDB: A0A0F0IIC8_ASPPU
Original site: A0A0F0IIC8_ASPPU 
ID   A0A0F0IIC8_ASPPU        Unreviewed;       478 AA.
AC   A0A0F0IIC8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=DadA {ECO:0000313|EMBL:KJK65618.1};
GN   ORFNames=P875_00010123 {ECO:0000313|EMBL:KJK65618.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK65618.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK65618.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJK65618.1}.
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DR   EMBL; JZEE01000360; KJK65618.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0IIC8; -.
DR   STRING; 1403190.A0A0F0IIC8; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
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   PANTHER; PTHR13847:SF279; DAO DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT   DOMAIN          54..431
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   478 AA;  52183 MW;  6CC1CF7A9B6922A0 CRC64;
     MQLPASNGTV AASAAETQPT GCFPVPNPGE CFWQTQPHPK SNHRSTEQLP DHSDIVIIGA
     GYAGISTAYH IVKDHKDFNK SITILEARGV CSGATGRNGG HLRPDFYGHI PTYIDRAGAR
     AGAEIAEFEI AHLPALKKVI EEEKIDCDFT LTRTIDVWCN EEAAAKAKAT FDSVVAQNFE
     YMNDAIFYTG KEVEGICGVK GAVACASYTA GTVWPYKFIM HLTESLLATG KVNLQTYTPA
     TSITPDSNGG YVIETPRGKM HAGNVIHANN AYVAGLLPEY EKNIIPCKGI CCRITVPEGT
     TAPLLNNSYI NRTEDNTLSY LIPRADGSII VGGAAAKFRS FREQWYNNVD DSVLIDSAKD
     YYTDYMQRTY RGWENSGAKV DKIWTGVMGY SYDSNPHVGE VPAKDGQFII AGFNGHGMPV
     IWLAAKELAK MVAQGTSFEE TTMPRLFKTT QFRIDRAKNG NEEDGDILGT GNFPATKQ
//
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