ID E2LR24_MONPE Unreviewed; 153 AA.
AC E2LR24;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
GN ORFNames=MPER_09413 {ECO:0000313|EMBL:EEB92127.1};
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:EEB92127.1, ECO:0000313|Proteomes:UP000000741};
RN [1] {ECO:0000313|EMBL:EEB92127.1, 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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:EEB92127.1}.
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DR EMBL; ABRE01014429; EEB92127.1; -; Genomic_DNA.
DR AlphaFoldDB; E2LR24; -.
DR STRING; 554373.E2LR24; -.
DR KEGG; mpr:MPER_09413; -.
DR HOGENOM; CLU_016755_4_3_1; -.
DR InParanoid; E2LR24; -.
DR OMA; CIAIRAS; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000000741; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000741}.
FT DOMAIN 13..148
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 153 AA; 16828 MW; CE1B35047E0DC518 CRC64;
MPPIYNKPTA DKYDYVIIGG GSGGSGSSRR AASYGKKVAV VEMTPHLGGT CVNVADLREK
LIYHAKGYKL EGLPDAPKFD WSSFKVQRDA YIRKLNGIYH SNFDKEGVEF HQGFGRLTSR
NTVEVTLPDG TNKYTLEADQ NRIATGGYQG EFG
//