ID A0A165SNN6_9APHY Unreviewed; 562 AA.
AC A0A165SNN6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KZT72265.1};
GN ORFNames=DAEQUDRAFT_763008 {ECO:0000313|EMBL:KZT72265.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT72265.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT72265.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT72265.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV429041; KZT72265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165SNN6; -.
DR STRING; 1314783.A0A165SNN6; -.
DR OrthoDB; 2086756at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.30.70.2450; -; 1.
DR Gene3D; 3.40.30.120; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR43004:SF6; FAD_NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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:UP000076727}.
FT DOMAIN 10..362
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 562 AA; 61597 MW; F6E1419D4E2A0135 CRC64;
MSADPASPGV LIGGAGPSGL VLALTLLTNG IPVRIIDKAR DFPLVQRGSG IQPRTLELFH
YLGTLSDMQA IYRPLLPVVE YKPGQVEPVK TSYMMEPVEP TPDVPYPNPI LLGQGYTQQI
LRAHLEKLGG AIETETELRH FGQTADGVTV TLVKQRNGEE VIETASFRWL VGTDGGKSGV
RKQLGLSFEG QALKEHSIHG ELYVEGLDAD HWHRWLDWQN PTIVTVVLCP TEVKGQFFFL
TGGHVNYSEL VEDQEKLLQA MRDFIKRDDI KLSNIRHAVE YRPQARIVEK YNLAVLMPAG
FYKMPHTCTA RREDRHGLNT SVQDAFNLGW KLALVEKGLA APSLLSTYSE ERLPVAKRMI
QETLGIYKVV MDSALQGANA SKARGAHIKQ LGVNYRWSPI VLDERNPVDK QQTVDALDVY
GKLGGDGVPR AGDRAPDAPG LVEVKQGSGA TRLFDIFGPT HHCVLIFCAD ASTARPVLEA
VQTLPPKTVT SVVIYPQTAS RKPPVAYADL VLADFEGHAF KVYGCPADST TIVITRPDGV
IGGTVFGDEG VKKYFKGIFS TV
//
