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Database: UniProt
Entry: A0A100IMH0_ASPNG
LinkDB: A0A100IMH0_ASPNG
Original site: A0A100IMH0_ASPNG 
ID   A0A100IMH0_ASPNG        Unreviewed;       647 AA.
AC   A0A100IMH0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   03-MAY-2023, entry version 22.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=ABL_06597 {ECO:0000313|EMBL:GAQ43936.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ43936.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ43936.1}.
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DR   EMBL; BCMY01000011; GAQ43936.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100IMH0; -.
DR   VEuPathDB; FungiDB:An19g00060; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1090102; -.
DR   VEuPathDB; FungiDB:ATCC64974_62930; -.
DR   VEuPathDB; FungiDB:M747DRAFT_273941; -.
DR   OMA; MDWIGPP; -.
DR   Proteomes; UP000068243; 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   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   PANTHER; PTHR42815; FAD-BINDING, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07600)-RELATED; 1.
DR   PANTHER; PTHR42815:SF2; FAD-BINDING, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07600)-RELATED; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          366..505
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   647 AA;  71579 MW;  26547D5D1AB44AD0 CRC64;
     MAISALQGWH PGEVAIQRQL GYATAVSSHW TAVENQLREQ HQIFHTSNLP FIALTTTDAD
     GRPWGGIVAG STGTVGFVDS PSLKSLVFRP RLWEGDPILP TLQGWRSLKD ITNHQMEGRR
     SEERSLTAGL GIEFPTRRRN KFAGKIHMVK AMSHYDYIFE VEITEALGNC PKYINVRQLD
     PFPWAKPHLV YQSLHMAPTE KLPPEVIDMI ESADTVFVAT IHRPDPTSAA MFPSHAGMNS
     RGGFPGFLRV RPSDRRSVVL PDYSGNRFMN SLGNIESSGL AGFTVISFTT GDILYLTGTA
     RNYVGPSALE IMSRHAAITV LSTTGFTLVR NALPVRQRKG SDVGRSPYTP KVKYLVEEGQ
     ADAGGAQGHK AILEKGMQLS DDLAIFRFEV ISKGDVRPLR IRPGQAIVLD FMDWIGPPPY
     QHMADSAPGS INDDRVRTWT VSSAHEDTDV AWFEITMREM KGGVVTKALF DVLRLSPPNR
     WDHPIFLEGD VVTEIVGVTG EFTLNKREAN LLLIAGGIGI TPFLAMLSAM STRENTPQGD
     IVLVLSTREP EVMLTLIEMA LHKVPSDVKV KVDLFTNCSV NLNTQILRHQ STSISIYEGR
     IGPEYWQTST RDKDVFICGP KAFADAAVDG LRTIGVPNER IEREGFY
//
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