ID A0A150VEE3_9PEZI Unreviewed; 812 AA.
AC A0A150VEE3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=M433DRAFT_131920 {ECO:0000313|EMBL:KYG48663.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG48663.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG48663.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG48663.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(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:KYG48663.1}.
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DR EMBL; JPDO01000042; KYG48663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VEE3; -.
DR STRING; 766039.A0A150VEE3; -.
DR Proteomes; UP000075602; 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:UP000075602}.
FT DOMAIN 343..603
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 157..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 89621 MW; F3D4C1BB9B883D74 CRC64;
MAQTTRREGS SMEYDTTIAS NAVRTTHNKS GFATFEQRWT TRQSSNTALI IRDPSGVNGG
SGSAYQIQSD SPWTVTPAYA AVASDLALQD DAHNGLTVLP YAHRQIVHSR PHSSFSFEQH
KHRSIPICAT SHPDNPIPIE PSDALLLSVT PQMRKKFNTM SSPRSSGESL EGITDDTTDS
DAPSTPLTEP QEMAEIIDQV HDLRASSPAK ARKRRASTTF ASNSEDIRKL LGSGSGTKFL
QKYCCGDGCC MAEALPAPEG QPEHIFITPP DNDAFRFLGL NLGSLTLSTE LTKIIDLPEQ
RVSFAAIRRE SITEKFPDEN THEHNRDAVN IYPPTYMKPH PPYSIFNAPV YGARELTKPG
AEKRTFHFDI DVTDYPEEGG VDFKVGGAVG VCPPNDPVVV EDIMDQLGIP RFQRDRPIRI
MTSGGRWPTI WGEDEARELV TTRREILTWT LDISSAPPTK PLFRLLAEHA EAENEKKILL
FLSSAQGQAA FCDLRTGPHV TLQQLLHAFP SSKPPLEKLC GVIPQLMPRF YSLSNDPYIS
SAREGLAGRR LIEIAVTIHE TLAYTGGKRT GVGSGFLESL ALKFIAAEKK AQEEAEAGHF
QTEPGIPGRR LNLQIPMFRG LMANPLSREF ASDGPMVLIG AGVGMAPFRG FILNRLKNAS
CANKIWLIQG IRDSMLDELY RGELGTHEKE IKKVVESRAH HDLPPVTSAE PDIAEQKDQN
LPAEVPFTSM KKQQKVAKYV QDEVRLQADI VWYVINAVDG RIFVCGSTKG MGEGVESALI
DVAMDKGNLD YETAKQFWKG KQEAGQYIAE TW
//
