ID N1QNK5_SPHMS Unreviewed; 356 AA.
AC N1QNK5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=SEPMUDRAFT_146768 {ECO:0000313|EMBL:EMF17838.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF17838.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF17838.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF17838.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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DR EMBL; KB456260; EMF17838.1; -; Genomic_DNA.
DR RefSeq; XP_016765959.1; XM_016903853.1.
DR AlphaFoldDB; N1QNK5; -.
DR STRING; 692275.N1QNK5; -.
DR GeneID; 27900990; -.
DR eggNOG; KOG0534; Eukaryota.
DR HOGENOM; CLU_003827_7_1_1; -.
DR OMA; WIDFFIP; -.
DR OrthoDB; 3060848at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00322; FNR_like; 1.
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; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR46505; OXIDOREDUCTASE NAD-BINDING DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR46505:SF1; OXIDOREDUCTASE NAD-BINDING DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF08030; NAD_binding_6; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT DOMAIN 67..189
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 39..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 39666 MW; 5948BE170EED8DB8 CRC64;
MLTRLGHYYR HYWPKAPSSL LSSPWKWKTS PGGISILPSR RRSMATINSS SSSIPHEQRT
QAEPREPQIE PVVLSHIRQI NDEIRLLRLS AVDPTHTIRF LPGQWVDTFL PTVRQAGGFT
ITSTPNEARP TSTRSSSSSS SSHSPPYLEL AVQKSKNPPA QWLWRPMEDI LGTQLAVRVG
GSFTWPPPPG LLDTSAIERL VLVAGGVGIN PLISIFTTLV RMPAQLRPPE MHFVYSTKTD
PDLDVQKILF MPRLMDAIAM AADPNVTLAA FLTGLGNEGI IEHGKLPNRT YGRRFQEEDL
VKALDGYKTS GFGPEHDRKN TVAYVCGPPK MTDEVVANLR SQPGMSDDRV LCEKWW
//
