ID B9RDV7_RICCO Unreviewed; 714 AA.
AC B9RDV7;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Ferric-chelate reductase, putative {ECO:0000313|EMBL:EEF50565.1};
DE EC=1.6.3.1 {ECO:0000313|EMBL:EEF50565.1};
GN ORFNames=RCOM_1616220 {ECO:0000313|EMBL:EEF50565.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; EQ973775; EEF50565.1; -; Genomic_DNA.
DR AlphaFoldDB; B9RDV7; -.
DR STRING; 3988.B9RDV7; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; B9RDV7; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IEA:UniProtKB-EC.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 2.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF41; FERRIC REDUCTION OXIDASE 2; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EEF50565.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 546..571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 591..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..430
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 714 AA; 80511 MW; 4A392B24B27C51D1 CRC64;
MVNSSPSSHK QTVDMLRAAI WILSVALLLG YLVLWIILPT NTYWRHWYGR IDEKFTSTYL
GRQGQPLLLF FFPILFIAVL GCAYIHLGKR SNQNILEGNG RKHRLAALRK PMLVKGPLGI
VSSIELAFLI MFIALLIWSL STYLHNSFST ITPQFAATRN ARVWEAKLES ASFLFGLVGN
ICLTFLFFPV VRGSSVLPLF GLTSEGSIKY HIWLGHMMMV LFTAHGIGYI IYWAVTNQIS
EVLKWGKTDV SNVAGEISLL AGLGLWATTF PRIRQKMFEL FFYTHHLYIL FMLFFILHIT
VGYSCIVMLP GFYLFLIDRY LRFLQSRTSV RLVSARILPC DTLELNFSKS PDFSYNPTSI
LFMNVPSISK LQWHPFTINS SSNLEPENLS IVIKSEGSWS KKLYHILSSP SSIDHLQVSV
EGPYGPASTH FLRHDTLVMV SGGSGITPFV SIIRELVYVS TTYKCKIPQV ILICSFKTSS
DLTMLDLLLP ISGTPSALSN LQLKIEAYVT REKEPTIDTS KLVRTIWFKP HSRDAPISAI
LGPKSWLWLG AIISSSVIIF LIIIGLITRY YIYPIDHNTW NVFSYSLEAV LYMLVISICI
AATASAAVLW NKRQNAREAK QIQIVEGSTP VRPLESGLCN GDRELESLPQ QPLVQVTNVH
YGKRPPLKRM LFEYKGSSVG VLVCGPKKMR HEVATICSSG SADNLHFEFI SFSW
//
