ID A0A2N6NL87_BEABA Unreviewed; 618 AA.
AC A0A2N6NL87;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Putative FAD-binding protein C12C2.03c {ECO:0000313|EMBL:PMB68039.1};
GN ORFNames=BM221_006215 {ECO:0000313|EMBL:PMB68039.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB68039.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB68039.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB68039.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:PMB68039.1}.
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DR EMBL; MRVG01000006; PMB68039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NL87; -.
DR OMA; LCCGGGC; -.
DR Proteomes; UP000235728; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000235728}.
FT DOMAIN 200..466
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 32..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 68516 MW; 7A0692AFCE3CBEBE CRC64;
MVQSPLATAA TKVLIASAGD CVPCEPSNAP SIAPSLTFSD ESDDAEEPAR PEKPRHRRAS
TRLIAQSARD IQRITGETTA EFVGRCCGGG CCLMGSQRPV GVDYEPLVLP DNAAFNSLGL
KFPEEIPTKL TAILDPPAKV VSFKSIPRPL SNPSDSGISM GPDGDTFSIT SVGNTSEPVK
LKSLDTSIQP PRFVQPHPPY HVYPAKIHTT RELTRDGAEK RTYHFDLDVT NYPDEESNDF
KVGGAIGVLA PNDDAVVDDV LDRLMVPHFV RDKQTLMTTT SGRWPTVWGD EKPRELVTTR
RDVLKWCTDL QSYPPTKNVF RVLAEHATDE VEKKVLLFLC SAQGQGTFCD IRTGPHVTVS
QLLYAFPSSQ PPLDELLSVL QQLMPRFYSL SNDPHDSYQI RDQKQHRLIE IAVTVHETSD
WRKGSRTGLG SGFFERQAQR FLQAQAVGEP NPEVYIPMFK GLMANPLAKE FNSDGPMLLI
GAGVGIAPFR GFVQRRLKQA NCANKVWVLQ GIRDSLVDEI YSGEWGVHEE EVKRVVQSRR
GEGRYVQEEV RNQADLVWYI ANSVDGRVFV CGSSQGMGEG VEEALIDVAM SKGNLERDEA
RNFWDLKKEA GQYIAETW
//
