ID E5AEL5_LEPMJ Unreviewed; 265 AA.
AC E5AEL5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Ferric reductase NAD binding domain-containing protein {ECO:0000259|Pfam:PF08030};
GN ORFNames=LEMA_P004410.1 {ECO:0000313|EMBL:CBY01654.1};
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|EMBL:CBY01654.1, 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; FP929139; CBY01654.1; -; Genomic_DNA.
DR RefSeq; XP_003845133.1; XM_003845085.1.
DR AlphaFoldDB; E5AEL5; -.
DR STRING; 985895.E5AEL5; -.
DR EnsemblFungi; CBY01654; CBY01654; LEMA_P004410.1.
DR GeneID; 13290660; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_0_2_1; -.
DR InParanoid; E5AEL5; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR11972:SF69; METALLOREDUCTASE AIM14-RELATED; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 45..241
FT /note="Ferric reductase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF08030"
FT REGION 72..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 265 AA; 30400 MW; 0311E27EEFAA5927 CRC64;
MQVHIKADGN WTNALRDIAE KGSNSTIKIG LDGPFGAPAQ RFYDYDYSMV FGAGIGVTPF
SGVLTDLQHH ELERVKPKSH SSSDASSETP REPSPYANHR RVDFHWQVRD KNNLLWFSDL
LNEVWRAQQL DSSNLDIRIN TYVTQKRKQI SEHVFRWLLE KHRTDEHPQS LITGLINPTH
FGRPDVKLIM EEHYSDMTKV LAERMNNEKD AKKKEQGDAE VKIGVFFCGP PVVGQQIADQ
CSQMTAKARN EGRNIEYRFM IEVFG
//
