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
//