GenomeNet

Database: UniProt
Entry: F8NZL2_SERL9
LinkDB: F8NZL2_SERL9
Original site: F8NZL2_SERL9 
ID   F8NZL2_SERL9            Unreviewed;       514 AA.
AC   F8NZL2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=FAD-dependent oxidoreductase 2 FAD binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SERLADRAFT_450323 {ECO:0000313|EMBL:EGO24032.1};
OS   Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=578457;
RN   [1] {ECO:0000313|EMBL:EGO24032.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S7.9 {ECO:0000313|EMBL:EGO24032.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA   Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA   Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA   Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA   Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA   Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "Evolution of plant cell wall degrading machinery underlies the functional
RT   diversity of forest fungi.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL945435; EGO24032.1; -; Genomic_DNA.
DR   RefSeq; XP_007319794.1; XM_007319732.1.
DR   AlphaFoldDB; F8NZL2; -.
DR   GeneID; 18816644; -.
DR   KEGG; sla:SERLADRAFT_450323; -.
DR   HOGENOM; CLU_011398_4_6_1; -.
DR   OrthoDB; 1132316at2759; -.
DR   Proteomes; UP000008064; Unassembled WGS sequence.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR040131; MnmG_N.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR43400:SF12; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          5..36
FT                   /note="MnmG N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01134"
FT   DOMAIN          85..490
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   COILED          368..395
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   514 AA;  55506 MW;  72DBF2552B47E15C CRC64;
     MTAYDCIVIG CGHAGSCAAL AAVESGCRKV LIVEKSPKEW AGGNGYFTAG AHRTVHNGLH
     DLLPIVNNVT VEQATLIDME PYTTENYIAD IMRLGNSQSD PILVKSMVDH SRDAVEWLAR
     HVGIPFILAF HRQAYEVGGR QKFWGGLALS VEDGGKGLIA AHLRALEKAG VEVWFDSPAV
     ELVMEDFAVR GVIVKKNGQK VQLSATAVIL AAGGYESSRQ LREKYLGPGW DRARVRGTPY
     NTGDGIAMAQ AIGAKLTGDW EGCHSTCWDA NAPADTGDRV MSNQFTKSGY PLGIMVNVKG
     DRFVDEGQDF RNYTYAKFGR AILQQPEGCA FQIFSGKIVE LLRKEEYADE IVEKIGASSL
     EELADKLVEK GLEEKENLLR TIREYNAAVR SHRAEYPGLL WDPSVRDGLS TQSSHSSLTL
     PKSNWALPLE DTPFVAVKVA CGITFTFGGL AIDPNTAGVL SEESGKPIKG LFCTGEMVGG
     LFYSNYPGGS GLTAGAVFGR KAGCEAASLV RDRS
//
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