ID A0A0M8MQQ1_9HYPO Unreviewed; 646 AA.
AC A0A0M8MQQ1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE SubName: Full=Putative FAD-binding protein {ECO:0000313|EMBL:KOS17356.1};
GN ORFNames=ESCO_006390 {ECO:0000313|EMBL:KOS17356.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS17356.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS17356.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS17356.1}.
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DR EMBL; LGSR01000026; KOS17356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8MQQ1; -.
DR STRING; 150374.A0A0M8MQQ1; -.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000053831; 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:UP000053831}.
FT DOMAIN 209..486
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 70602 MW; 07996A45DFFB0E84 CRC64;
MSTLQTTHSL PSAVDGGVPE TQKAPSSAAP SLSLSSDDSA DDQDNEPLHR RRASTKLIAQ
NARDIQRITG ETTAEFVGRC CGGGCCLMAP PGSKRRAGLE YEQLVLPDND AFRALRLNIT
EIPTVLSKIA PLPPKLVSFS PIRRPASPSS PTDSAISLGS DGDALRSMAT ANDMDRCTKK
TLARESGNTD GGVDTSIQPP SFVQPHPPYH VFPARIHSAR ELTNPGAEKR TFHFDLDVSD
YPDEEKIEFK VGGAIGVTAP NDDALVQDVL DALMVPHYAR DRPVRMATTG GRWPTVWGEE
EARELVTTRR DVLTWCADLQ SYPPTKPLLR VLAEHAADDN ERKILMFLCA AEGQATFCDL
RTGPHITVPQ LLHAFPSSCP PLDELLSCLQ QLMPRFYSLS NDPHESFQIR DQKRHRLIEV
AVTVHETDDW RGGKRTGVGS GYFERQARRF LAAQKASAAA ASAEAGAAGA AGADQARGPP
ELFIPMFKGL MANPLAQQFN ADGPMLLIGA GVGIAPFRGF VQRRLKQANC ANKVWVLQGI
RDSLLDELYS GEWGVHEEDL KRVVQSRRGE GKYVQEEVRH QADLVWTIIN AVDGRIFVCG
SSKGMGEGVE QSLVDVAMAK GNLQRDEAHT FWNLKKEAGQ YIAETW
//
