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Database: UniProt
Entry: R7QHP7_CHOCR
LinkDB: R7QHP7_CHOCR
Original site: R7QHP7_CHOCR 
ID   R7QHP7_CHOCR            Unreviewed;       613 AA.
AC   R7QHP7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   03-MAY-2023, entry version 39.
DE   SubName: Full=NADPH-dependent diflavin oxidoreductase NDOR {ECO:0000313|EMBL:CDF36971.1};
GN   ORFNames=CHC_T00009367001 {ECO:0000313|EMBL:CDF36971.1};
OS   Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Gigartinaceae; Chondrus.
OX   NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF36971.1, ECO:0000313|Proteomes:UP000012073};
RN   [1] {ECO:0000313|Proteomes:UP000012073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX   PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA   Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA   Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA   Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA   Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA   Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA   Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA   Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA   Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA   Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA   Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA   Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT   "Genome structure and metabolic features in the red seaweed Chondrus
RT   crispus shed light on evolution of the Archaeplastida.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
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; HG001808; CDF36971.1; -; Genomic_DNA.
DR   RefSeq; XP_005716790.1; XM_005716733.1.
DR   AlphaFoldDB; R7QHP7; -.
DR   STRING; 2769.R7QHP7; -.
DR   EnsemblPlants; CDF36971; CDF36971; CHC_T00009367001.
DR   GeneID; 17324502; -.
DR   Gramene; CDF36971; CDF36971; CHC_T00009367001.
DR   KEGG; ccp:CHC_T00009367001; -.
DR   OMA; DIMSIPR; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000012073; Unassembled WGS sequence.
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   4: Predicted;
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012073}.
FT   DOMAIN          8..157
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          217..466
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   613 AA;  67510 MW;  7310DEBDFE032E66 CRC64;
     MTADASPVHV LYATATGTAE DVAQSLSESL AARGTLIKSC TTVDEYNIAS LPVHSSQGHR
     FIFIIATCGD GEVPLSMRKF WHFIRRADLP GGILAEMRFA IFGLGDRAYV KFNAAARKLH
     LRLQDLGAAP FASLALGDDS AQGGYDKELM PWFASVCQAV VPKSHTNTNY TDRRGEVIEP
     RICVHLVDKG KGTLSGSAAT NIWKSGQAEL SDSIAVGDLH ESHVLKNDII TDAAFLSDDK
     EVRHIELDVS KAPAKSGLLD YIPGDIVHVM PRNRASAVDA FFQLTGFDEN AVVRVEQSHT
     KKRFGSYTLN VQQPCVLREF VSAQLDLSCM PRRRFFERLA PFAADAMQQE KLIEFASADG
     ADILTQYAYR EKRTILMVLR DFPSARPPLD HLVDMIPVLK SRAFSIASSQ QAHAGQIHIC
     ASIVRYTTPL KFARVGVCSS FFLNLGVGDV VPIFLEKGTS LRFKESKPSI MLGPGTGVAP
     MRSFISSSKP NVNGNTLFFG CRSRRGDFLY EKEWEQYQAS GQFSSLVTAF SRERAGAKVY
     VQDKLLEECE NIWTLVAKKE AHVYVAGAAG AMPKSVRLAL VEICQRSGGL SEIESNSYVR
     QMEVDGRLQM ECW
//
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