ID Q0V3V3_PHANO Unreviewed; 471 AA.
AC Q0V3V3;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=SNOG_01311 {ECO:0000313|EMBL:EAT90960.1};
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:EAT90960.1, 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 -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; CH445326; EAT90960.1; -; Genomic_DNA.
DR RefSeq; XP_001791955.1; XM_001791903.1.
DR AlphaFoldDB; Q0V3V3; -.
DR STRING; 321614.Q0V3V3; -.
DR EnsemblFungi; SNOT_01311; SNOT_01311; SNOG_01311.
DR GeneID; 5968800; -.
DR KEGG; pno:SNOG_01311; -.
DR VEuPathDB; FungiDB:JI435_013110; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_5_1; -.
DR InParanoid; Q0V3V3; -.
DR OMA; WPQYAVH; -.
DR OrthoDB; 1770094at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR Gene3D; 3.30.9.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789:SF268; 5-METHYLPHENAZINE-1-CARBOXYLATE 1-MONOOXYGENASE; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF01494; FAD_binding_3; 2.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
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}.
FT DOMAIN 29..273
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 325..396
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 471 AA; 51879 MW; E5C228B2B395BE04 CRC64;
MRRPSFLFPD PHCFHGFTIA MPYLESQPKI IIAGAGIGGL TAALALHASG FTNIQIYEAS
SQLTTLGVGI NVQPSAVLIL RNLGLLEALE KTGIQTRELN FYNRHGDSIL SEKRGVAAGY
AVPQFSIHRG EFQMLLLSAV KERLGNDALH LNHALTGFEQ NEKTITAQFS QRRDGVPAAQ
SSVTGDILVA ADGINSTARR ILYPNEGPPK FSGCMLWRGC IERDQYLTGA SMVWAGHADQ
KFIAYPISRR SADKGKSLVN WIAELRIREK DDEDTTPPKT DWTKSVNKDV FAGPFESWRC
GGLEMKDLID STEKVFEFPM SDRDPVEHWT FGRLTLLGDS AHAMYPIGSN GASQAIIDAE
TLAKHLSSTT SSSTTIEEAL KAYEQERLPP TAKIVMANRA NGPDHVLQLA EERAPDGFEN
VYDVIPKEEL EEVGRIYKKV AGFEIESVND KAKKTEGEST RLGLKSPSDW I
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