ID   A0A0G0IP23_9BACT        Unreviewed;       435 AA.
AC   A0A0G0IP23;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Ferric reductase like protein transmembrane component family {ECO:0000313|EMBL:KKQ25924.1};
GN   ORFNames=US39_C0003G0024 {ECO:0000313|EMBL:KKQ25924.1};
OS   Microgenomates group bacterium GW2011_GWC1_37_12b.
OC   Bacteria.
OX   NCBI_TaxID=1618510 {ECO:0000313|EMBL:KKQ25924.1, ECO:0000313|Proteomes:UP000034251};
RN   [1] {ECO:0000313|EMBL:KKQ25924.1, ECO:0000313|Proteomes:UP000034251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KKQ25924.1}.
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DR   EMBL; LBSU01000003; KKQ25924.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0IP23; -.
DR   STRING; 1618510.US39_C0003G0024; -.
DR   Proteomes; UP000034251; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd06198; FNR_like_3; 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; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
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   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        41..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        85..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          210..309
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   435 AA;  48722 MW;  709A1A62179B72E6 CRC64;
     MLNYLSLSRH NIGNYVIIGL TLIPLLFWYP HANVSGVNNI FLATGQVLGL MGSVLFSLNF
     MLSARLRFLE KYFGGLNRIY IIHHIIGAIA LIFLLYHPVM ISLFYLPLSV VAAAKILFAG
     PSNVPVFLGL TALAVLIIAL VLTFFIKLPY QIWKLSHKFL GLSLFLASLH IYLIPSTVSV
     SLPLRIYILG ISVVGIAAYL YRSIFDKLLI RKYKYKVEAV NKLGNDVTEA VMSPLEKPMN
     YLPGQFIFIN FESLGITRET HPFSLTSSPD TPQLSLGIKS SGDYTETIKL LKKDAVAEIE
     GPFGYFTFYR YGTNRQIWIA GGIGVTPFIS MARSLAMPNP YRIDMYYVVS TADEAVYQKE
     LEKIAAQISG FKLFPHFSKT MGRFNTESLA KSSPDFVGAD IFLCGPPPMM KSLKDQLKKV
     KVKGYRIHSE EFSID
//