ID A0A067K461_JATCU Unreviewed; 719 AA.
AC A0A067K461;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=JCGZ_19157 {ECO:0000313|EMBL:KDP29818.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP29818.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP29818.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP29818.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KK914730; KDP29818.1; -; Genomic_DNA.
DR RefSeq; XP_012081586.1; XM_012226196.1.
DR AlphaFoldDB; A0A067K461; -.
DR Proteomes; UP000027138; Unassembled WGS sequence.
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:SF69; METALLOREDUCTASE AIM14-RELATED; 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:UP000027138};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 597..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..444
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 719 AA; 80089 MW; E9D77FB8A365D6AE CRC64;
MDKHSTQELL LSNGNLQTTD YVSKKAVVFS LILKWILKIA MLAAFIAWLT VVFMYPIKSF
QTWLKNWNQA FADSFLGFTG GVFLIFNGPL IIIALLSIPY LTLCSREEEL QKKEGAKGRG
HRLWTSPVVV DGPFGVVSAA EFIGILVFLG YIAWVACIYA VQKISVIFTN PEYTIEDKWS
WTFRSARGFG LVGIFCLAFL FIPVVRSSLL LCLVNIPSEH AIRYHIWLGH LCMLLFTFHG
LFYVIGWFMS GEIPSELIAW DATDGANLAG IINIFFGWSI WITSLPFVRR KIFELFYYAH
HLYIIFIIFL AMHVGNFFMC IPAGAIFLFM VDRFLRFCQS QKTVDVVSTK CFPCGVVELV
LSAPTTTGLI NYNALGSLFL GIPQLSLLQS HPFSVSSSPL DGKNRISLLI KAAGDWTNGL
KDNVETNNKI RASVEGPYGN RLPYHLMYEN LVLVAGGIGI SPFIAVLSDV IHRINQGKTC
LPRNITLVWA VKKSDELSLL STINTNSLVP LPFDVLHLEI LIYVTREQES PMTERSASSI
SSFSSENAIS ALVSTGNKTW FGAYVISSTV GLVLLMTLLN VFYITPFNIT NWWHQGLLLL
ACMVGGVVIF GGAVVALWHI WEKRNLVEIN GGQGNEHTVN EDSFLENLAG STTVQYGSRP
DFKEIFGSIS RLWGDVDVGV IVCGPPNLES SVAAECRSIN MGRKSDDPVF HFNSHSFSF
//
