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Database: UniProt
Entry: A0A183R9A5_9TREM
LinkDB: A0A183R9A5_9TREM
Original site: A0A183R9A5_9TREM 
ID   A0A183R9A5_9TREM        Unreviewed;       711 AA.
AC   A0A183R9A5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=NADPH-dependent diflavin oxidoreductase 1 {ECO:0008006|Google:ProtNLM};
OS   Schistosoma rodhaini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0001256601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SROB_0001256601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   AlphaFoldDB; A0A183R9A5; -.
DR   STRING; 6188.A0A183R9A5; -.
DR   WBParaSite; SROB_0001256601-mRNA-1; SROB_0001256601-mRNA-1; SROB_0001256601.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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; 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   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}.
FT   DOMAIN          19..194
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          275..543
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   711 AA;  80683 MW;  0239A65103153DA3 CRC64;
     MLPQTNHSIS CPTTTDKSIT ILYGSQTGNA QSLAESLALQ SYRIFDQECV KSNLERLPIT
     RLLSMDDYTP VSRLAKEKGV MIFVCSTTGH GVPPNNMSLF WKKIMNRALI PGRSLPPDLH
     FSVLGLGDSS YPMFNFVAKK LYRRLLQLGA TPLCTEIRPH QDCEESENLS LGLADEQSEL
     GINEVLRYWI PALWDNVMKL FGVPTSERLS RLISWDNLKN PDFVFSLWPK YDVICSSLVL
     NPGLQSTSEN NLLHQIVKQV EFDNAHSFMS NPIPTNAQWF QVVRCRRVTS ADHFQDTRLL
     EMSYKPDIDL KSDEFRLGSV LYVQPTNRKE DILSFFQITR LNPTERVKIT QCHPNFPVPN
     LLRALEENDC DVSIAWLATY YFDLNATPQQ CFFVNYCAFA VSCLKLSKSL DRAQHIDKDR
     LKLEVDRLTD LASAANSDDI DDLYDYVFRP CRRVVEVLAD FPVTSSLLTL QYILDILPGP
     ILARPYSVAS PPPKIELLVA VVNYRTRLST PRIGTASNYL ASLNPGDCFS GWLGTISGGF
     KFDRLLTLSP PSCLLIATGT GIAPFHSFLL HQYNSLKSHL NHDTIPTNVL FFGCRYSTKD
     YYFASDFKML EEKGWLRIIP AFSRENTSTV SPSRRQYVQD QLKNYPEIVW SILKSPQSHI
     FIVGNQKTMP DEVREALLYA IVNANHMDSS GAEVLLGQME TENRIQIESW T
//
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