ID F1L239_ASCSU Unreviewed; 588 AA.
AC F1L239;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE SubName: Full=NADPH-dependent diflavin oxidoreductase 1 {ECO:0000313|EMBL:ADY44193.1};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY44193.1};
RN [1] {ECO:0000313|EMBL:ADY44193.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; JI169915; ADY44193.1; -; mRNA.
DR AlphaFoldDB; F1L239; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.360; -; 1.
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; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
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:SF10; NADPH-DEPENDENT DIFLAVIN OXIDOREDUCTASE 1; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 2: Evidence at transcript level;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 4..148
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 196..440
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 588 AA; 66751 MW; BF793820F3ACAB8F CRC64;
MDSLLIVYAT ETGTAQDTAE SLSHDAKYRN IRARVLSLED YNIENLCNER CAVFVVATSG
QGEMPSSIRA NWKKLCHKSL SHETLAGVYI AVLALGDSSY QRYNFAGKKM FRRLRQLGAV
PLIDLALADD QHELGIDATL DDFRDALFRR IAEMNLFEGI SMVFDESKCL PPRYELCFED
APEMIPLSSN SMKSTAGFTK ATVKVNRRVT ATDHFQDTRL VSIASMDGDH PLSYKPGDVL
MVHPFNLHET LSIALDALGY TEAVLDRKFR AVPTDTNIPS LPEWLLDGYT SLRMCLERYF
DLQIVPRRSF FKILSKLSTF EAEKERLLEL ASAEGLDDYL NYCVRPKRTI AETLRDFGCT
ARSIPPERLF DLLPTIRARA FSIASCPKTH GTVQLLVAKV EYRTKRMVEP RRGLCSSYIS
RLCPGDEIFV KVRPGTFRWP SEDCSLILVG PGTGVAPFRA ILNYRCSLKR EEEMASSLLF
FGCRGEKKDF YFADEWPLLH STRVITAFSR DNPQKKVYVQ NKIREYADTV WDLLEHNNGF
VFVAGRADNM PNDVMEQFKK IASSKGVDGE RYFASLESKG RVQFETWN
//
