ID F8P3G0_SERL9 Unreviewed; 547 AA.
AC F8P3G0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=SERLADRAFT_416705 {ECO:0000313|EMBL:EGO22060.1};
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:EGO22060.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO22060.1};
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.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; GL945437; EGO22060.1; -; Genomic_DNA.
DR RefSeq; XP_007320598.1; XM_007320536.1.
DR AlphaFoldDB; F8P3G0; -.
DR GeneID; 18813519; -.
DR KEGG; sla:SERLADRAFT_416705; -.
DR HOGENOM; CLU_009665_20_3_1; -.
DR OrthoDB; 2086756at2759; -.
DR Proteomes; UP000008064; 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; 3.40.30.20; -; 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 InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_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.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 8..346
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 547 AA; 60328 MW; 960ED59505A54E18 CRC64;
MTLSLDNTPV LIAGAGPSGL VAALTLLKNG IAVRIIDKEP KHRIGQRGAA IAPRSLELYH
FLGVDEIEKN ANPPPLVRTY RPGGLEPLET LPIAVHVDPT PAYPYFNFAM LGQDCAESHL
HSHLAKYSCY VEFGTELVSI EQHPDHVRAH LVKKRDDREI LETAQVSCEG SLGDIRVKGL
DNKVWSSNLV IAFVMLNCLQ HWHMWGDMST NLVALRATPD FGEDGFALFA SGHGLDTERI
ASNHDLLIDF LTSVTERQDM HFDVRWASDF RPNIRMTRRF RDGRVFLAGD AAHVHSPTGG
QGMNSSIQDT FNLGWKLALV IKGLAPPSLL DTYSEERIPV IAEMLKVTTE LLDDTAKADR
STTGSAFKRD PSMYQLGVNY RGSSILVDEQ DLLENEVDPY GLVTEGSLQA GDRAPDSTGL
HVVGPPDEEG ITRLFAVFKP WFHTALIFTK DSSDVRMLTS ALRRYPQGTI RCVVLSPRGS
SVSRAAAGDL HLVDGEGHAF KWYNVPEEGG RVVVVRPDGV VGAIVHGVEG LHRYFELIFF
SVDRILV
//
