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Database: UniProt
Entry: E5AEU3_LEPMJ
LinkDB: E5AEU3_LEPMJ
Original site: E5AEU3_LEPMJ 
ID   E5AEU3_LEPMJ            Unreviewed;       558 AA.
AC   E5AEU3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Amine oxidase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LEMA_P005190.1 {ECO:0000313|EMBL:CBY01732.1};
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:CBY01732.1, 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).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00043981}.
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DR   EMBL; FP929139; CBY01732.1; -; Genomic_DNA.
DR   RefSeq; XP_003845211.1; XM_003845163.1.
DR   AlphaFoldDB; E5AEU3; -.
DR   STRING; 985895.E5AEU3; -.
DR   EnsemblFungi; CBY01732; CBY01732; LEMA_P005190.1.
DR   GeneID; 13290812; -.
DR   eggNOG; ENOG502SIR2; Eukaryota.
DR   HOGENOM; CLU_028280_0_0_1; -.
DR   InParanoid; E5AEU3; -.
DR   OMA; NFQTTLW; -.
DR   OrthoDB; 1771364at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   Gene3D; 1.10.405.20; -; 1.
DR   Gene3D; 3.30.70.1990; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR42923:SF26; FMN REDUCTASE LOT6, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G06600)-RELATED; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..558
FT                   /note="Amine oxidase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003195272"
SQ   SEQUENCE   558 AA;  60224 MW;  0D135E0EC991AC4D CRC64;
     MPPITTLFAL PLRLLLLVSA ILPQSITATP SILTTDVVIL GGGASGTYAA VRLRDDLNTS
     ILLIEPHSHL GGSVSTYRVA GTNESFEYGV QSYLPNGPAL ALFTRFGIAL EPFTANRLSA
     LNVDIETGRV LTDYTAPSAN ATNAAFGRWL EVVAKYEHML EPGYWDFPQP GHVPAVLLES
     FGVFAKREGI EAAVPRIMAI SGVGSGGIQG LLVLHVFQAF GASLTRDVLS NSLVKPVGSN
     SLLYERALAR LQPDVLLEST VQDVRRTSAG VELWVKQGSR EYLIQARRVL YAAPPSLSNL
     GPFHPDEKEK AVFEQWAEGG EYIGVAKIDC IPEGVSVNFF PKSASPSNYL ALKDYPYSLR
     LDSTGPPGMH LFRVIFGANF TLTAGIFKDL VADSVQKLQD GGAVTGRCET DFKAVSNHSR
     PMWKQSAEQI QAGFVQDLYG LQGHRGMWGM EIMKRVFDAT DKDSKIVWLA HTIPSLSQAT
     VLHKSGKKKI RCGFCLDGLG PNAQVPLSLQ GGMPAEKDGR LRLRLELMCG GGVTMVMVTI
     WVTVRSAMGA GGCTLSCI
//
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