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Database: UniProt
Entry: B2AC79_PODAN
LinkDB: B2AC79_PODAN
Original site: B2AC79_PODAN 
ID   B2AC79_PODAN            Unreviewed;       664 AA.
AC   B2AC79;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 3, supercontig 1 {ECO:0000313|EMBL:CAP61044.1};
GN   ORFNames=PODANS_3_150 {ECO:0000313|EMBL:CAP61044.1};
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:CAP61044.1};
RN   [1] {ECO:0000313|EMBL:CAP61044.1, 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}, and S mat+
RC   {ECO:0000313|EMBL:CAP61044.1};
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|EMBL:CAP61044.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP61044.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {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).
RN   [4] {ECO:0000313|EMBL:CDP26495.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., 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   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; CU633448; CAP61044.1; -; Genomic_DNA.
DR   EMBL; FO904938; CDP26495.1; -; Genomic_DNA.
DR   RefSeq; XP_001903272.1; XM_001903237.1.
DR   AlphaFoldDB; B2AC79; -.
DR   GeneID; 6187496; -.
DR   KEGG; pan:PODANSg284; -.
DR   VEuPathDB; FungiDB:PODANS_3_150; -.
DR   eggNOG; ENOG502QUV4; Eukaryota.
DR   HOGENOM; CLU_018354_4_2_1; -.
DR   OrthoDB; 1641938at2759; -.
DR   Proteomes; UP000001197; Chromosome 3.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 2.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR13878:SF176; FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..664
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007638530"
FT   DOMAIN          194..373
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   664 AA;  71827 MW;  37C959C4D6990B9B CRC64;
     MIAVSLSRAL LLAGTFARLG LAQTEPTILA EDGSVLSANE TTVAPAAEVE VVGDAGEVLL
     LTDAVLANLT ALDLSDINLF TFDEDVSGVT TKRSFSRGFQ VGDCKVFPGD RAWPSRLSWT
     VFNLLTGGAL IETVPIGAVC YPNSGVYNAA KCQYVLANWA QSALHASDPT SVMSPLYQGE
     TCMPQNGQTG TCEMGSFPSY SVKIHSVYQV QLAVNFARNQ NLRLVVHNTG HDFLGKSTGA
     GALSIWTHNL KDIKYVKSFR SPSYNGPALK LGAGVQVGEL YAAANSLGVT AVGGECPGVG
     VAGGYLAGGG HSPLSSKYGL GSDQVLSIDV VLPNGRFVTA TETKNTDLFW ALRGGGGGTF
     GVVTSITVKV HPKQKFAGFS MTLNAGPESE NSIAVFWQAM YAYWRKFPDY AAQGVYGYST
     VFPLFTAAGG YSWTFHPFMM PNMTLAQFKV HVQPLLNEWT AMGLAFTPNF FEKDNLYDVW
     TQYFPAESVA NSNMRTASRM FPASVWNNST NRDALFDEMR AIVEEGSALI QYNMNPRQTE
     GTPNSAANSH WRDAIWFAIM GAGWAPGTPE PELAATNNKI THDWMERLRA WGPGGYGNEG
     DVMEPNFGEA FFGTNYQRLL SIKREVDPND LFWAPTAVGA ERWTIQGQPS WLTTQVGKLC
     KISN
//
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