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Database: UniProt
Entry: B2B492_PODAN
LinkDB: B2B492_PODAN
Original site: B2B492_PODAN 
ID   B2B492_PODAN            Unreviewed;       888 AA.
AC   B2B492;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 2, supercontig 2 {ECO:0000313|EMBL:CAP72616.1};
GN   ORFNames=PODANS_2_480 {ECO:0000313|EMBL:CAP72616.1};
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:CAP72616.1};
RN   [1] {ECO:0000313|EMBL:CAP72616.1, 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:CAP72616.1};
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:CAP72616.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP72616.1};
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:CDP25011.1}
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 (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ADIP family.
CC       {ECO:0000256|ARBA:ARBA00009291}.
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DR   EMBL; CU640366; CAP72616.1; -; Genomic_DNA.
DR   EMBL; FO904937; CDP25011.1; -; Genomic_DNA.
DR   RefSeq; XP_001910792.1; XM_001910757.1.
DR   AlphaFoldDB; B2B492; -.
DR   GeneID; 6196153; -.
DR   KEGG; pan:PODANSg7833; -.
DR   VEuPathDB; FungiDB:PODANS_2_480; -.
DR   eggNOG; ENOG502RZ1J; Eukaryota.
DR   HOGENOM; CLU_010128_0_1_1; -.
DR   InParanoid; B2B492; -.
DR   OrthoDB; 2726628at2759; -.
DR   Proteomes; UP000001197; Chromosome 2.
DR   InterPro; IPR021622; Afadin/alpha-actinin-bd.
DR   Pfam; PF11559; ADIP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT   REGION          187..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          774..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          74..136
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        194..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..414
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..487
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..605
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..655
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..748
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..867
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   888 AA;  96947 MW;  7209D6ED8B1A6312 CRC64;
     MIVSENLRTA SLYINNQLLS RGLLRDGQNI DFTNPGESEE EMGETMSRIM SVVNDLILRR
     DRDAEHRESL SATLRTLRAE SLRQANDIQR LQEKNAEAQR KAGLSDAAET ALRAHIKTAE
     ATIHRLKEEA ARTKLLAAQT RSACATEVRK RDRQIEGLKK AVSEAARARG ASKSPGVTSI
     TVVGDIGADE QGNPLPPTPT TTASSSDGYD LRQETNSFLA ELAKGLSEEN EGLLTLIRRT
     TEQLKDMSGW DAGMVDSDGY ALSLPTGYDD MAAEIEAVLE HLRTILTNPS FVPIEEVVVR
     EDEINRLRDG WEKMETRWKE AVHLIDGWRR RMQASGRPVN VEELKMGLRL SPVKVQNVEE
     TAQGGLGLQL ESVHEGHESY HHDQVDYQDE DEGPLELVPE GGIEEQDDSD TSSVFEDQQI
     DMDELDVEEP NVEILQQSVV MPSPPVAPAP QPSPLREHFS AGNKGGRDGP NLRRRPKFAE
     EGVRSRPLSE ESPLPPPHAD RPQQSPSKKP LLSVRTVPSE ETGTAAQPPS AAVSTPDTSI
     SLDSVSLPKA AAAEPKSAVT KKSAPTPPPH ATRPIKKPSP APRPVKETRK PPSRQQEREE
     RKTSTTSTTT TRQQQQESEA RQKKVTSRPP VTRPTRPPIT RGRSETRKGD SDTSKPSKPT
     ARNTSATSTT STRSAPVSSS SKTSIPPNPE PAPGKSPRRV NSRLPLPRNA GSSGSNNSAC
     AAGTATNNAP VLQPPQSPTQ AQQSPLSMAT IQAKLAASER DADAARVRAK LKAARKGIHL
     PGPGSGRVTA ENSMPNTPTE TMSTKSMRSE QSDYIQYQPE QYDDGEDELG FSAVQPHQVI
     HAEKPRKRER NYGEAVAARK TSDKVASRRR STLNPWELET LIKGGNAE
//
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