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Database: UniProt
Entry: A0A0A1TMF0_9HYPO
LinkDB: A0A0A1TMF0_9HYPO
Original site: A0A0A1TMF0_9HYPO 
ID   A0A0A1TMF0_9HYPO        Unreviewed;       496 AA.
AC   A0A0A1TMF0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VHEMI08011 {ECO:0000313|EMBL:CEJ92355.1};
OS   [Torrubiella] hemipterigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX   NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ92355.1, ECO:0000313|Proteomes:UP000039046};
RN   [1] {ECO:0000313|EMBL:CEJ92355.1, ECO:0000313|Proteomes:UP000039046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA   Hertweck C., Linde J.;
RT   "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT   Verticillium hemipterigenum.";
RL   Genome Announc. 3:e01439-e01414(2015).
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; CDHN01000004; CEJ92355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1TMF0; -.
DR   OrthoDB; 2041362at2759; -.
DR   Proteomes; UP000039046; 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   PRINTS; PR00411; PNDRDTASEI.
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:UP000039046}.
SQ   SEQUENCE   496 AA;  56494 MW;  B16C7607E75DF718 CRC64;
     MESQKLDALI VGAGFGGVYQ LKKLRDAGFH VKLIESGSDY GGVWYWNRYP GARVDSAIPV
     YEFSDPALWK DWHWTQRFPG SAEIRAYFKT VADKWDLRKD TEFNTYVNSA IWNDESKTWR
     VSTANGKVFT TQFFLPNTGF AAKRHTPDFK GIDRFKGTWV HSSYWPKEEP YLKGRKIAVI
     GTGSTGLQLT QDLAPLASEF VLFQRTPNLA LPMKQEEYPP GSETQCIPGE AYPALFAGRA
     ESYAGFDFSF MPVKTFDHDE KERQETYQKL WDHGDFRFWL ATYQDMLFDD RANTEAYNFW
     RDKVRARLDD ERLKDKFAPM EKPHAFGCKR VSLENGFYEL FNKKNVHLVD VNETPITEVT
     PAGIKTTEKE WEFDYIVCAT GFDAITGGIL QMNVEGINGL KLKDKWMDGT KTFLGLSVAD
     FPNMFFTYGP QAPTAFCNGP SCAELQGTWI VDLLSSMRQK KQEVVNASAE AEKTWAESIW
     AIANTSLIPT TKSVCS
//
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