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};
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 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
//