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Database: UniProt
Entry: A0A1S4E038_CUCME
LinkDB: A0A1S4E038_CUCME
Original site: A0A1S4E038_CUCME 
ID   A0A1S4E038_CUCME        Unreviewed;       490 AA.
AC   A0A1S4E038;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=NADPH-dependent diflavin oxidoreductase 1 isoform X2 {ECO:0000313|RefSeq:XP_016901574.1};
GN   Name=LOC103494455 {ECO:0000313|RefSeq:XP_016901574.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_016901574.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA   Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|RefSeq:XP_016901574.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   RefSeq; XP_016901574.1; XM_017046085.1.
DR   AlphaFoldDB; A0A1S4E038; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000089565; Unplaced.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd06207; CyPoR_like; 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000089565}.
FT   DOMAIN          90..335
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   490 AA;  55876 MW;  E0794AF2051EE764 CRC64;
     MLYDRYEAAL DPWMLSLWSS LNDINPMFFL KGTDFVFSND TIIDQPSVQV AYYNMGKLDS
     PLTSDLKCTE IQIERARLMS PGKFSHGKKK PDCFLKMIKN QCLSKVGSGK DVRHFEFEFV
     SSVIEYEVGD VLEVLPSQSS AAVNAFIQRC NLDPESFITV SPRNRRKQDP ILAAEMGPVK
     LKTFIELTMD ISSASPRRYF FEVMSYYATA PHEKERLQYF ASPEGRDDLY QYNQKERRSV
     LEVLEDFPSV KMPFDWLVQL VPPLKTRSFS ISSSALAHPN QVHLTVNVVS WMTPYKRKRS
     GLCSSWLAGL DPEQCVHVPV WFHKGSLPAP APSLPLILVG PGTGCAPFRG FVEERSIENT
     SMATAPVLFF FGCRNEDNDF LYRDFWLSHS ENHGVLSEEK GGGFYVAFSR DQPRKVYVQH
     KMLEQSEKIW NLLREGAAVY VAGSSTKMPA DVWSTFEEII SKETQLPRES AVRWLRALEK
     AGKYHVEAWS
//
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