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Database: UniProt
Entry: A0A0D0BKI5_9AGAM
LinkDB: A0A0D0BKI5_9AGAM
Original site: A0A0D0BKI5_9AGAM 
ID   A0A0D0BKI5_9AGAM        Unreviewed;       560 AA.
AC   A0A0D0BKI5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=CY34DRAFT_800471 {ECO:0000313|EMBL:KIK46462.1};
OS   Suillus luteus UH-Slu-Lm8-n1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX   NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK46462.1, ECO:0000313|Proteomes:UP000054485};
RN   [1] {ECO:0000313|EMBL:KIK46462.1, ECO:0000313|Proteomes:UP000054485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK46462.1,
RC   ECO:0000313|Proteomes:UP000054485};
RG   DOE Joint Genome Institute;
RA   Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
RA   Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
RA   LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
RA   Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KN835159; KIK46462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0BKI5; -.
DR   STRING; 930992.A0A0D0BKI5; -.
DR   HOGENOM; CLU_005646_3_0_1; -.
DR   InParanoid; A0A0D0BKI5; -.
DR   OrthoDB; 367877at2759; -.
DR   Proteomes; UP000054485; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:monoatomic ion transport; 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; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR000778; Cyt_b245_heavy_chain.
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:SF39; FAD-BINDING FR-TYPE DOMAIN-CONTAINING PROTEIN; 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   PRINTS; PR00466; GP91PHOX.
DR   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR   SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 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   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054485};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          236..380
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   560 AA;  64260 MW;  3F54A3F94605D111 CRC64;
     MGESWFQSEF LNPRRLVFNV IFYGIQVTLF ALGWYLQATN TKLAALNALK WSVWTSRGAG
     LTLAFDAGLL LVPMLRNVIR VVRPKLTWLF PADENIWFHR QVAYSMAFWA MVHTTAHYVN
     FFNVERTQVR PEYALQIHYT QAGGITGHFM LLIMVLMYAT AHHKIRNQCF EAFWYTHHLA
     FFFFIGLYTH ATGCFVRDTA NPDYISTFPF YSTEHCLGYE SWRFTIWPGI IYFGERMYRE
     YRARRATRLS KVLVHPSGAM ELRIIKPSFK YTAGQWLFIQ VPEVSRWQWH PFTITSAPED
     PYVSVHIRQV GDWTHSLGER LGCGPSVVAA MTKVAMGGVE KDETKYGGTR GEYVELDPAT
     LSRPLPQVRI DGPYGAPAED VFDNEVAVLI GAGIGVTPFA SILKHIWYRQ KKGNLGSLRR
     VEFFWVCRDA PSFGWFQSLL QEVEEAQVDP NFLRINIYLT QKIGEDMLWN IAVNDAGADY
     DPLTLLRTRT MFGRPDWKSI YRRIREAIEI GQYLPGSSAQ LKTKVGTYFC GPGVLAKSIK
     AATLMHSSNN VNFTFAKEHF
//
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