ID A0A090CEQ7_PODAN Unreviewed; 420 AA.
AC A0A090CEQ7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CDP26466.1, ECO:0000313|Proteomes:UP000001197};
RN [1] {ECO:0000313|EMBL:CDP26466.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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DR EMBL; FO904937; CDP26466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090CEQ7; -.
DR eggNOG; KOG2614; Eukaryota.
DR InParanoid; A0A090CEQ7; -.
DR Proteomes; UP000001197; Chromosome 2.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.9.60; -; 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; PTHR47469; MONOOXYGENASE-LIKE; 1.
DR PANTHER; PTHR47469:SF2; OS06G0597600 PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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:UP000001197}.
FT DOMAIN 124..257
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 420 AA; 46516 MW; 400C968D2F886D05 CRC64;
MPKSVIIVGG SIAGLLHGIY LKRHGANVII LEQDPNPRRS SHNAGICFGP SVQEFLRLYN
DTGIQACQPA VVTRLAYRQN LYWRDTGIVR HLTSWGVLYR ILRANFDGLA SDAVTIPPPA
RAGDGQCSYL PGQRVTSVQK TSDGVVVGYL GEDGKERCSV ADLVIGADGL HSTVRGLLNA
PVVKEYSGYV SWRGTVCEAK VSPETARYFQ DRTVLSLLKR TYIVCYIIPP DSGSFAPGTR
LINWVWYCNL SETPETNFAE LLTDTNGHLH ANTVPSGLVR AEIWKSHLAH MLPLIPGPFA
ELFTQTEQPF ITKVNDALCS KATFFDGRVL LVGDALATFR PHFALATEQA ARHCLGLARV
WKGEISLQLW EREAVDHAIK IWLGSRVMGA GLLRGWVEFL LLAWKYVVFF ARSKLGWNRV
//
