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Database: UniProt
Entry: A0A2J6TAA3_9HELO
LinkDB: A0A2J6TAA3_9HELO
Original site: A0A2J6TAA3_9HELO 
ID   A0A2J6TAA3_9HELO        Unreviewed;       535 AA.
AC   A0A2J6TAA3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:PMD59955.1};
GN   ORFNames=K444DRAFT_529455 {ECO:0000313|EMBL:PMD59955.1};
OS   Hyaloscypha bicolor E.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX   NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD59955.1, ECO:0000313|Proteomes:UP000235371};
RN   [1] {ECO:0000313|EMBL:PMD59955.1, ECO:0000313|Proteomes:UP000235371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E {ECO:0000313|EMBL:PMD59955.1,
RC   ECO:0000313|Proteomes:UP000235371};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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DR   EMBL; KZ613803; PMD59955.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6TAA3; -.
DR   InParanoid; A0A2J6TAA3; -.
DR   OrthoDB; 2041362at2759; -.
DR   Proteomes; UP000235371; 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; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235371}.
SQ   SEQUENCE   535 AA;  60810 MW;  966003EC2D829C28 CRC64;
     MGSVEQQQYD AIVVGAGFGG CHVLRTLRER GYKSIVLDNA ADIGGVWYWN RYPGARVDSK
     VPLYEFSDKD LWGDWSWSVK YPGQNEIQEY FQHVESKLHL KKDIRFNTTV TTANFDDINN
     QWHVHTNDGS VFVSRFFILC TGSFSEPYIP KFEGLDTFAG PKFHTSAWPH GGIDYKNKRV
     AVVGNASSGL QTIQEIAPDV SHLTVFQRSP TFAIPMRQTK LNSKDQDKSK YPQIFESRKN
     NFAGIDRQFN PQSALEVSDE ERTKFFEELW EQGGLLFWLA TYQDVIMNKE ANKYAYAFWR
     SKVLPRIKKP EVAEILAPEV PPYFFGTKRA TLEQRYYEVY NQDNVVLINT RENAIKYVVP
     QGIIREDNTF HELDILVLAT GFDSVTGGLL AIDIKGLKGQ TLREKWAHGT WTSLGVMTSG
     FPNMFFTYGP QGPTTFCNGP TCAELQGEWV VSSMDFMREK GHTFLNPDVG SEKAWREHVN
     MIGNMSLLPL TESEYMGTNI PGKTKEMLNY LGGLPSYVQK CNDLLASGFE GFDIK
//
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