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Database: UniProt
Entry: B2AQU7_PODAN
LinkDB: B2AQU7_PODAN
Original site: B2AQU7_PODAN 
ID   B2AQU7_PODAN            Unreviewed;       515 AA.
AC   B2AQU7;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   13-SEP-2023, entry version 54.
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 4, supercontig 4 {ECO:0000313|EMBL:CAP66525.1};
GN   ORFNames=PODANS_4_3120 {ECO:0000313|EMBL:CAP66525.1};
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:CAP66525.1};
RN   [1] {ECO:0000313|EMBL:CAP66525.1, 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:CAP66525.1};
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:CAP66525.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP66525.1};
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:CDP28255.1}
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.
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DR   EMBL; CU633895; CAP66525.1; -; Genomic_DNA.
DR   EMBL; FO904939; CDP28255.1; -; Genomic_DNA.
DR   RefSeq; XP_001905859.1; XM_001905824.1.
DR   AlphaFoldDB; B2AQU7; -.
DR   STRING; 515849.B2AQU7; -.
DR   GeneID; 6190606; -.
DR   KEGG; pan:PODANSg2887; -.
DR   VEuPathDB; FungiDB:PODANS_4_3120; -.
DR   eggNOG; ENOG502S6Z4; Eukaryota.
DR   HOGENOM; CLU_029647_0_0_1; -.
DR   OrthoDB; 1469611at2759; -.
DR   Proteomes; UP000001197; Chromosome 4.
DR   InterPro; IPR037393; Bud22/SRFB1.
DR   InterPro; IPR015158; Bud22_dom.
DR   PANTHER; PTHR23325; SERUM RESPONSE FACTOR-BINDING; 1.
DR   PANTHER; PTHR23325:SF1; SERUM RESPONSE FACTOR-BINDING PROTEIN 1; 1.
DR   Pfam; PF09073; BUD22; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT   DOMAIN          24..256
FT                   /note="Bud22"
FT                   /evidence="ECO:0000259|Pfam:PF09073"
FT   DOMAIN          261..515
FT                   /note="Bud22"
FT                   /evidence="ECO:0000259|Pfam:PF09073"
FT   REGION          31..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..231
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..280
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..324
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  57889 MW;  467D3DB02D20B549 CRC64;
     MVKRKRGDDD SSLNVSAVFF KHRDEVFRAI KNAKGRERQR QSKRLKDAKS TPDKKARIEK
     EIVVLNVGFD RYSCERRYMI LMQVQSLDLH QTAHAHLCSS LLRVKSIAEH EKLPNEIKSG
     VPKPELTEEE RAALHNVTSA LYSHAGVKEA VAKALEDVCK ALGVSVPEKK GRGKKERLEE
     KEGVKETSEP KKAKSDKKEK KEKDTKQDKV KDLPVADDSE EEDEDINYGE DVDETVVSRM
     ADLLGSSSED EDDEGEKMKL AKRQTKTKKA LPKELDPMEI TSDEEGGDEA DSDDDSDDDL
     DPMQITDDEA DEENDNEESE DEFGGFSDSN QSSASDSDSE EEKEEEDQQS DASSSAQSPP
     PKKSKRAAKV EVNGSTFLPS LMGGYISGSE SASDVDLAPT RKNRRGQRAR QAIWEKKFKE
     QAKHLKKQQE KRDSGWDLKR GAVDGDNKPW KKGIKNPFKA TGANDVAVKK EEEPPKKDRK
     RDDLGTLHPS WEARRLAKEK EKLTAPFEGK KITFD
//
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