ID Q0URG5_PHANO Unreviewed; 537 AA.
AC Q0URG5;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_05649 {ECO:0000313|EMBL:EAT86713.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT86713.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH445332; EAT86713.2; -; Genomic_DNA.
DR RefSeq; XP_001796047.1; XM_001795995.1.
DR AlphaFoldDB; Q0URG5; -.
DR EnsemblFungi; SNOT_05649; SNOT_05649; SNOG_05649.
DR GeneID; 5972924; -.
DR KEGG; pno:SNOG_05649; -.
DR VEuPathDB; FungiDB:JI435_056490; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006937_8_0_1; -.
DR InParanoid; Q0URG5; -.
DR OrthoDB; 2041362at2759; -.
DR Proteomes; UP000001055; 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; 3.
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:UP000001055}.
SQ SEQUENCE 537 AA; 61140 MW; AEC047B5A74AD887 CRC64;
MGSIDELKAH YPNDNSNGTH TEDLDALIVG AGFGGVYQLK VLRDAGYRVK LVEHGSDYGG
VWYWNRYPGA RVDSEIPHYE FSDPALWEDW TWKQRFPGSE ELRAYFAYVA KKWDLRKDTQ
FNTFVSSATW NDGQGRWTVN TEAGEIYKAK YLLLNTGFAA KRYIPDWKGV DSFEGTFLHP
SYWPHEELEL AGKRIAIIGT GSTGIQLAQE LSKVASHLTV FQRTPNMSLP MGQAEFNAPK
QAIPKPKYPD LYAKRTDSFS GFNFNFLPRA TFDDTPEQRQ STYEELWSKG DFHFWLATYH
DMLFRKDANH EAYKFWRDKT RAKINHPKIA DILAPMEQPH AFGCKRISLE NKYFEIYNQP
NVTLVDISNK GTPIQEITEK GIKTAGLEYE FDFIVSATGY DAITGGLTQI DIKGTSGESL
SDHWKDGAKT YLGLAVSNFP NMFFTYGPQA PTALCNGPTC AELQGNWILQ AMKHLDDKGL
KKIEVEKDSE DEYKKWYMGT NIPNKPREPL IWLGGVPEYY KMINNSAADG YNGFKLS
//