ID E2LRR0_MONPE Unreviewed; 227 AA.
AC E2LRR0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
DE Flags: Fragment;
GN ORFNames=MPER_09678 {ECO:0000313|EMBL:EEB91891.1};
OS Moniliophthora perniciosa (strain FA553 / isolate CP02) (Witches'-broom
OS disease fungus) (Marasmius perniciosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=554373 {ECO:0000313|EMBL:EEB91891.1, ECO:0000313|Proteomes:UP000000741};
RN [1] {ECO:0000313|EMBL:EEB91891.1, ECO:0000313|Proteomes:UP000000741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FA553 / isolate CP02 {ECO:0000313|Proteomes:UP000000741};
RX PubMed=19019209; DOI=10.1186/1471-2164-9-548;
RA Mondego J.M., Carazzolle M.F., Costa G.G., Formighieri E.F., Parizzi L.P.,
RA Rincones J., Cotomacci C., Carraro D.M., Cunha A.F., Carrer H., Vidal R.O.,
RA Estrela R.C., Garcia O., Thomazella D.P., de Oliveira B.V., Pires A.B.,
RA Rio M.C., Araujo M.R., de Moraes M.H., Castro L.A., Gramacho K.P.,
RA Goncalves M.S., Neto J.P., Neto A.G., Barbosa L.V., Guiltinan M.J.,
RA Bailey B.A., Meinhardt L.W., Cascardo J.C., Pereira G.A.;
RT "A genome survey of Moniliophthora perniciosa gives new insights into
RT Witches' broom disease of cacao.";
RL BMC Genomics 9:548-548(2008).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEB91891.1}.
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DR EMBL; ABRE01014713; EEB91891.1; -; Genomic_DNA.
DR STRING; 554373.E2LRR0; -.
DR KEGG; mpr:MPER_09678; -.
DR HOGENOM; CLU_1264248_0_0_1; -.
DR InParanoid; E2LRR0; -.
DR OMA; VAYPISH; -.
DR OrthoDB; 1947085at2759; -.
DR Proteomes; UP000000741; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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; PTHR46720; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR PANTHER; PTHR46720:SF3; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000741}.
FT DOMAIN 108..174
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEB91891.1"
SQ SEQUENCE 227 AA; 25966 MW; 475DCA4020197BE7 CRC64;
RTLLTEKSRW AHSEGRYKEA AELMHSVDPA XSGTIAYRAL IPSERLRARY LSHRTLTTPM
QYLGKGGYVI AYPISQGKLV NFVAFTFRHD LENTKYNGPW VSSSDKSQRR VAVMGDAAHA
AQPHQGSGAG QAIEDGYILA IVLGHPRTTR ENVHRALRIY DEIRRPMAHR VQENTRQNGR
YYSFELDGID LDQLDPDEQW DILQRMGKKF VKNWEWVDDA VQKQSGD
//
