ID A0A161Y6Z7_DAUCS Unreviewed; 724 AA.
AC A0A161Y6Z7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=DCAR_025204 {ECO:0000313|EMBL:KZM88129.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM88129.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM88129.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM88129.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZM88129.1}.
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DR EMBL; LNRQ01000007; KZM88129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161Y6Z7; -.
DR EnsemblPlants; KZM88129; KZM88129; DCAR_025204.
DR Gramene; KZM88129; KZM88129; DCAR_025204.
DR OMA; MTRYYIY; -.
DR Proteomes; UP000077755; Chromosome 7.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 532..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 310..415
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 724 AA; 81528 MW; 60E718F3F5642009 CRC64;
MEPKRIQAMI KMAVMLVFLG YVFIWVILPT NLYKKDWLLK IRAKTMSTYF GTQGATMLVN
TSPMLLIAVL GCVYLHFMHK ARGKDIQGKQ GSDALRRPMI IKGLGIVNGI ELSFFIMFIA
LLIWSFSAYL EISFAKITAK SAAKSGEKVW QAKLDSAALR LGLIGNICLA FLFFPVTRGS
SVLPLLGVTS EASVKYHIWL GHIVMTLFTA HGVCYIVYWA VTNQLSEMLK WAKTDVSNVA
GELALLFGLV MWVTTIPGIR RKMFELFFYV HHLYILFMVF FVYHVGFSYA CIMLPGFYLF
LVDRFLRFLQ SRQRVRLVSA RLLPCETVEL NFSKSQGLNY TPTSIMFVNV PSISKVQWHP
FTVTSNNNLE PEKISIVIKG DGSWSKRLFH TLSAPSAIDR LDVSIEGPYG PAATNFLRHD
ALVMVSGGSG ITPFISIFRE LVFLSETLKC KTPKILLISS FKNSSDLTLL DLLLPISDTP
SNFSNLQLQI EAYVTREKQS SPTNNKDNIR SIWFKPRPSD STVTPILGQN TWLWLGTIIS
SSFILFLILL GTLNRFYIYP IDHNSNDVYS YSAKGTISML LLCISITVTA TGAFLWNKNQ
NAMETKQIQN MEGTTPMASP DSQFYNADRE LESLPQQSLV QSTNVYYGER PDLKRYLFER
KESRVGVLVC GPKKMRHEVA GICSSGLADN LHFESISFSW PVNPEGNEVV KGLIENATYK
TVVV
//
