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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//