ID S8DJ29_9LAMI Unreviewed; 679 AA.
AC S8DJ29;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Ferric-chelate reductase {ECO:0000313|EMBL:EPS59492.1};
DE Flags: Fragment;
GN ORFNames=M569_15311 {ECO:0000313|EMBL:EPS59492.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS59492.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS59492.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
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:EPS59492.1}.
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DR EMBL; AUSU01008323; EPS59492.1; -; Genomic_DNA.
DR AlphaFoldDB; S8DJ29; -.
DR OrthoDB; 2671609at2759; -.
DR Proteomes; UP000015453; 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: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:UP000015453};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 514..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 296..401
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPS59492.1"
SQ SEQUENCE 679 AA; 76851 MW; E6070392096C95E5 CRC64;
VLAAGYFSLF VMMPISQYFH VWIPKLRSHT SSTYFGTTQG SAYFLLYTVP VLLISLLGCF
YLHLGKNKGT TAGRRRRWET WRRPIVVMRG LGIVSRIELS LLIMFIALLG WNLGRFLATD
FRNITIAPNS HTHHRWQARL ERAAVRLGLV GNISLTFLFF PVTRGSSVLR IFGLTSESSI
RYHMWLGHIA MGLFTAHGFC YILYWAVTHQ SSEIVRWSKT GVSNIAGEIS LAAGLGLWAA
TVPGFRRRFF NVFFYSHHLY ILFVVFFVFH LGITFATIML PGFYLFVVDR YVRFLQSRRR
LGILCARVLP CDTVELTVAK TRTLDYAPTS ILFLNIPMIS KLQWHPFTIS SSSNLEADKL
SIAVKAEGFW TKKLYELVSS HPSIDRLQVS IEGPYGPTST PFLRHDILVM ISGGSGITPF
ISIIRELIHK SQNPQQRIPQ VLLICAFKNS SDLTMLDLIL PVSNSGFSNL QLKIEAFVTR
EKHPAQDPKA IRTVWFNPDS SDEPMSPVLG QNSWLWLAAI ISASFVVYLI FIGILTRFYI
YPIDHNSNNV YPLGWRSLFH MSFICICIVI ASTAAFLWTK SSNAQIQHTQ GLTPQISPVS
RSYNAAAIEL ESLTLQSLSQ SVNVHHGERP DLRKILLEHK EQNTGVLVSG PQKLRHEVAK
ICSSRLAANL HFESISFSW
//
