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Database: UniProt
Entry: A0A178AJR9_9PLEO
LinkDB: A0A178AJR9_9PLEO
Original site: A0A178AJR9_9PLEO 
ID   A0A178AJR9_9PLEO        Unreviewed;       518 AA.
AC   A0A178AJR9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:OAK97783.1};
GN   ORFNames=IQ06DRAFT_379601 {ECO:0000313|EMBL:OAK97783.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK97783.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK97783.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK97783.1,
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; KV441717; OAK97783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178AJR9; -.
DR   InParanoid; A0A178AJR9; -.
DR   OrthoDB; 445965at2759; -.
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; 1.
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:SF304; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
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}.
SQ   SEQUENCE   518 AA;  57926 MW;  E9C6809F5C32B101 CRC64;
     MAVTVAIIGL GAGGLVSLKN LREQGFDVTG FERSSHIGGL WRYSDSDQLS VLSTTVVNIS
     KERGCFTDFP YPDSVPSYPT AAQVHEYLLS YVKHFNLEPH FRLNAPIQQV IFDDDRQQWV
     VKIEGESDKY FDKVLVAIGG MVGQPNMPSI EGLDKFQGKS IHSRYFKRPE DFSGKRVMVV
     GFGNSAADTA TQLVGLASKI YLAHRHGAHI LPRILNGAPI DHTHALRLFN LQVLIIKYFP
     HAGERFFENF VKGLQNKRFK LRPEWGFEPA QKIPIVSDTL VEHLEAGDIE STKGVKRIVG
     STIVELDDGR HVDVDAIVWC TGYKSDFSII DPRFDPTAAP TEAWSAAQGS NGKSMFNLYQ
     NVFSAEKPDS LAFIGNVHFT ISGFQIFDMA SMAVAQVWKG NSQLPSSEQI KREVSAHHEW
     LADLASRGYN VSPGNVDAGP WMRAMDDLGG MGVNEYLGYG WKGWRFWLSN MRFCNLLMGG
     IWSPCIYRAF EGKRERWDGA KEAIESVNAK KQETMKSK
//
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