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Database: UniProt
Entry: E5A5S0_LEPMJ
LinkDB: E5A5S0_LEPMJ
Original site: E5A5S0_LEPMJ 
ID   E5A5S0_LEPMJ            Unreviewed;       389 AA.
AC   E5A5S0;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Similar to monooxygenase FAD-binding protein {ECO:0000313|EMBL:CBX98968.1};
GN   ORFNames=LEMA_P082070.1 {ECO:0000313|EMBL:CBX98968.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
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DR   EMBL; FP929134; CBX98968.1; -; Genomic_DNA.
DR   RefSeq; XP_003842447.1; XM_003842399.1.
DR   AlphaFoldDB; E5A5S0; -.
DR   STRING; 985895.E5A5S0; -.
DR   EnsemblFungi; CBX98968; CBX98968; LEMA_P082070.1.
DR   GeneID; 13286872; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_009665_3_0_1; -.
DR   InParanoid; E5A5S0; -.
DR   OMA; IHERGEN; -.
DR   OrthoDB; 1776894at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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; PTHR47178:SF5; FAD_BINDING_3 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47178; MONOOXYGENASE, FAD-BINDING; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:CBX98968.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT   DOMAIN          127..365
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   389 AA;  43341 MW;  DE614D97CB8503AA CRC64;
     MAENSNNPHV LIIGGGLAGL ALAQALRAQN YTFQMFERDI SEVGRTQGWC ITLNGDMLDS
     FAQYFPSDMP DLAQVDHLCG TGIETSSAVY HASKNVLKEL IRFGSKLGDR QIRANRGRLR
     SWLMTNISVQ WGKQFERYEE DANGVTAYFK DGSQFHGDIL VGADGIHSRV RAQILPVVHP
     GFLPMGAICG EIEAPKEQYE RWMQLGTSWV SAFSDDLRVT YLVSSVSEDR NIAKLYWLFG
     WQDEDALKDD FWTSKASREE MHQFVLSRLH KLHPQIAEPF QATPVEGMVL PPLRLCDMLP
     PVLPAGRITL VGDAAHSMTP FRGQGGNVAM ADAISLARSI HERGENQSLS DVLKLYEEEM
     RPRAMVKVLE SRAGAYEANA QPKKEANGS
//
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