ID A0A0C9X807_9AGAR Unreviewed; 1054 AA.
AC A0A0C9X807;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=K443DRAFT_128287 {ECO:0000313|EMBL:KIK08365.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK08365.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK08365.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK08365.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler 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., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KN838542; KIK08365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9X807; -.
DR STRING; 1095629.A0A0C9X807; -.
DR HOGENOM; CLU_003662_0_0_1; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000054477; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06207; CyPoR_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054477}.
FT DOMAIN 669..900
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1054 AA; 115127 MW; 003D7CE09A7FE4C8 CRC64;
MSLNGSGWST PISSTTTLSS PPSPYPKKIA IPKSLYENYH IPAYHLVEHI ASRSRTSSSV
YLYDVAEQVG FGTLTDKWSK TGKEIASVIK LQTRAGGGLG LIGRLSQGTS HDAGSNAVLT
AYTTPAGLAS MASSFAYLPP ATSFSRLVIQ VPAVTSTGEA LALSPSLASL AAVWPILPNN
VAVLFSATPQ QTLDFAAISY QLTNWHTIHL FDHYSSSREV GHSLTAPPDP EDHGDSVHDV
MCRAGYSFFE YSGDSEAVTV VVLLNSLLAL KIKTFVTSQQ INGLGVVIVN VLRPWDEATL
QSILPFSVKA VHVLDDVPNP VTQGNLYVDV FSALWDGTNS RSVYAHRATP SQHQLYLGND
NSFLQFFNTF APTRVERPLA GPSSLRKLLI FDTPYSSLSV VPQAIEELFL NRGMVARLLT
DYDAFSKSGG VSAHRILLAS KSNLTSVPPV AMTLPLDPLS SGEADFLAVL DQSLLKSHLL
LQHAKPNSTI LVDTSWTNIE FSHNLPADQI KSIVERNLTV FAIDSSHLAA NLAGAPGPAR
DAVQNLIVHL AILRLYLGPG AEEAAVLKVA QNEYGEAVEG ISLLKINAHA WSGLRIVEIE
TSSLPVSSNA SPLLKNFESN AITVDQNVEG VIQTGRIGSW HDAAKHFLFP ATYSPSAQPL
RALRPEIPDH TYLVTCTVNK RLTPLEYDRN VFHLEFDTAG TELKYSIGEA LGVHGWNDEA
EVLDFCAWYG VDHNRLITIP VASEEQKMHT RTVLQALQQQ VDLFGRPPKS FYSDLAEYAT
SSVDRHALLF IGSPDGSSTF KKMSEKDTLT FADVLKKYPS AKPGVEKLCE LIGDIKPRHY
SIASAQSVVG DRVDLLVVTV DWKDSNGRKR YGQCTRYLAG LRVGQKVTVS IKPSVMKLPP
NPKQPIIMAG LGTGAAPFRA FLQHLAWLAR KGEEIGPVYY YFGSRHQASE YLYGEEIEAF
VLDGIISRAG LAFSRDSAKK VYIQHKMLED SEALAHMLHD DEGVFYLCGP TWPVPDVYEA
LVNALVKYKG SDSVAAGEYL ESLKEKERYV LEVY
//
