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Database: UniProt
Entry: A0A178ALZ9_9PLEO
LinkDB: A0A178ALZ9_9PLEO
Original site: A0A178ALZ9_9PLEO 
ID   A0A178ALZ9_9PLEO        Unreviewed;       484 AA.
AC   A0A178ALZ9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:OAK98631.1};
GN   ORFNames=IQ06DRAFT_278042 {ECO:0000313|EMBL:OAK98631.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK98631.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK98631.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK98631.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; KV441715; OAK98631.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178ALZ9; -.
DR   InParanoid; A0A178ALZ9; -.
DR   OrthoDB; 2453855at2759; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 2.
DR   PIRSF; PIRSF000332; FMO; 3.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT   REGION          65..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   484 AA;  54103 MW;  A53A4A2D8D2C7E24 CRC64;
     MTAKRVAIIG LGPGGAIAID ALAQEKAFET IRVFERREAP GGCWLEDESP PPNLEASTLP
     ALAARNADGP IPIPSNLPTS TPPSQKARYA ESSVYPYLET NVDSRTMSYS QELIPAGASP
     LSVAKHGEDT PFRHHSIVRK HIESLINRNG YEKFVSYNTA VELAEKVGDE WRLVLRKSNK
     ADAKDEWWEE RFDAVIVASG HFNVPYIPHI NGLADLERAH PGSVKHSKMF RGRDAYRGKR
     VVVVGASVSA ADIAYDVVGI ARGPVYAVIL GHKANGYFGD VAFQHPGITQ KPSISHITTE
     NGDRTVHFVD GTAVREVDEI IFGTGYTWSL PFLPHVKVRN NRVPGLYQHV VYQDDPTLLF
     VGAVSAGLTF KVFEWQSVLA ARILAGRATL PSLEEQRRWE QDRIAKKGDG VAFTLLFPDF
     EQYFNEVREL AGEPKHGEPG RRLPLFKKEW FEVFMAGHER RKKWWREENE RARLKVAEPV
     RAQL
//
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