ID W8C881_CERCA Unreviewed; 592 AA.
AC W8C881;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE SubName: Full=NADPH-dependent diflavin oxidoreductase 1 {ECO:0000313|EMBL:JAB98924.1};
DE Flags: Fragment;
GN Name=NDOR1 {ECO:0000313|EMBL:JAB98924.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB98924.1};
RN [1] {ECO:0000313|EMBL:JAB98924.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB98924.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
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; GAMC01007631; JAB98924.1; -; mRNA.
DR AlphaFoldDB; W8C881; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase 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 HAMAP; MF_03178; NDOR1; 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; IPR028879; NDOR1.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 16..160
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 205..444
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB98924.1"
SQ SEQUENCE 592 AA; 67770 MW; BB217C4AA19C142B CRC64;
KLKKKIINRA IAKMRMVVLY GSQTGTAQNV AERIWRESKT WGFSGPVLPM DEYPVQQLIE
EKLAIFVVAT TGNGDEPDNM RKTWKFLLRR SLPVDSLRYL KFACLGLGDS SYAKFNFAAK
KLNKRLIQLG GHAIQPLGLC DDQHDHGLGA TALPWITQLF NVTLLPFHPS KCSGKAKNIF
KWNVNCLEPE MALFKDSMPK WFLSSEAISL TLKENRRTTH VEHFQDVRFL RFDFPSDVKW
NAGDVLELVP SNSDEQVLKF FELVKEHNLD FNEKTIVKLE SAYDDMPVPF VYAAPISVGM
LAKYVWDLSA CPNQRAFEVL SLNCEDEMEK EKLEEFATIE GLEYLINYVN RPRRTILEVL
QDFRHSTSKL KLPNLFEMFT VIQPRSFSIA SMPTTLSLDL LVAVVEYKTK MSTKRLGLCS
NWLKSLPTGS TVVGVIKNGT MSLPSEPSTP IIMVGPGTGI APFRSVIQYR KEQQNTGAKI
GDLIVFFGCR NKTKDYHFSE DFSNWQKENF CETFVAFSRD QERKVYVQHL IKEQKERLSE
LIMDKMAVIL VAGSSNNMPK AVREAFIEVI NGNEEYLEHM IKSRRYQEET WS
//
