ID E5A564_LEPMJ Unreviewed; 599 AA.
AC E5A564;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Amine oxidase domain-containing protein {ECO:0000259|Pfam:PF01593};
GN ORFNames=LEMA_P080010.1 {ECO:0000313|EMBL:CBX98762.1};
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; CBX98762.1; -; Genomic_DNA.
DR RefSeq; XP_003842241.1; XM_003842193.1.
DR AlphaFoldDB; E5A564; -.
DR STRING; 985895.E5A564; -.
DR EnsemblFungi; CBX98762; CBX98762; LEMA_P080010.1.
DR GeneID; 13282207; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_7_1_1; -.
DR InParanoid; E5A564; -.
DR OMA; YVTFPRA; -.
DR OrthoDB; 2642916at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF404; POLYAMINE OXIDASE FMS1; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 72..585
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 384..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 66431 MW; BB7FD97861E72D3D CRC64;
MEDTLRPNVE YRTFIPNNRS SFLATSVSRM QRDLSCSLHQ VGPLEVKEDV TAPMIRRVAG
KVPHVCVVGA GVAGLRCADV LLQHGLKVTI LEGRDRVGGR ICKSLSSPQV WTHSCIKSIT
NAVYRSGPNW IHGTDNNPIL DLARETNTRV MNWDGRQAVF DHLGNLMPEP EAAENTEHVW
TIIERAMKLS NDDSASIPAE KSLYDFFKEQ VVEMFPPDDE GEGKAKSKQN TILQMGEMWG
AFVGSPVQSQ SLKFFWMEEC IDGENLFVAE TYHKVLEKIA EPALKATVKF GHVVKEIVSS
ITDQGNGTSV TVKIEGQQSQ TYDEVVITAP LGWLKRNLHV FKPELPARLK AGIDSISYGH
LDKVYINFPT AFWNDKSFQE TTATSRVKDH SVPNGTATAA PHHQNQDEES VSATINPKHW
PGFTHWAAPS YAEHTNPLRW NQEAVNLAAL PGSTAHPTLL FYIFGPTSLH IAKMLASNPE
SKHQELLTEF FHPYFSRLPN YSANDPAHQP KAVLATAWAN DELSGYGSYC NFQVGLEKGD
EDIETMRQGM PERGVWLAGE HTAPFVALGT VTGAYWSGEG VAKRIVKAYG IDAVNERKA
//
