ID E5A279_LEPMJ Unreviewed; 510 AA.
AC E5A279;
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 FAD binding domain containing protein {ECO:0000313|EMBL:CBX97956.1};
GN ORFNames=LEMA_P093650.1 {ECO:0000313|EMBL:CBX97956.1};
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).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; FP929132; CBX97956.1; -; Genomic_DNA.
DR RefSeq; XP_003841435.1; XM_003841387.1.
DR AlphaFoldDB; E5A279; -.
DR STRING; 985895.E5A279; -.
DR EnsemblFungi; CBX97956; CBX97956; LEMA_P093650.1.
DR GeneID; 13281318; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_1_2_1; -.
DR InParanoid; E5A279; -.
DR OMA; TYTIPYI; -.
DR OrthoDB; 2446456at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF27; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..510
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003193304"
FT DOMAIN 65..237
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 510 AA; 54956 MW; 71FABEBF2046079A CRC64;
MEAIIRLTLA TLLLTARSAS AAPSPDTTQA CSEIKQALPG KVLEPQLLAL EYAFEKQQYW
STSLRTVDPA CIVQPVDAND VSVVVKILNK YPEVKFATRS GGHDPNVGHA TVQDGVLITM
TDIVGATYDA QNHVAYVKPG GEWNDVISDL EPSGVTIAGG RLGLVGVGGL LLGGGLSFLS
AQEGLAADNI IGWETVMANG SIVNVDAKAH PDLAQAMRGG GSQFGIVTKF TVNVHPIGDV
WGGSCAYDPT QDDKLYAALH QYAGNGSAAD PKSGIIFTDL VAAAGVTTKI IYYFYDGPTR
PTSGPFADFF KIPGLACLPR KQKYSELLKA NGEPVRLLNA RSFFRTLTVP FIPSRPQMYS
EIRSKLKSTV SPFLNLPPVV RGVQFSVDFQ PLPSIIGTHS AAKGGNAMGL TASDPERIII
IFQGAWNLAF DDELVNGFAK EMTDWLAEQV PRWLDEAGMP RDVYLPLFLN DAQSDQQVMQ
SYSGYERFRE LQKSVDPNGL FSSRAGGFKF
//
