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Database: UniProt
Entry: B2AQD7_PODAN
LinkDB: B2AQD7_PODAN
Original site: B2AQD7_PODAN 
ID   B2AQD7_PODAN            Unreviewed;       412 AA.
AC   B2AQD7;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   08-NOV-2023, entry version 72.
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 4, supercontig 4 {ECO:0000313|EMBL:CAP67077.1};
GN   ORFNames=PODANS_4_4490 {ECO:0000313|EMBL:CAP67077.1};
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:CAP67077.1};
RN   [1] {ECO:0000313|EMBL:CAP67077.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP67077.1};
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:CAP67077.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP67077.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; CU633895; CAP67077.1; -; Genomic_DNA.
DR   RefSeq; XP_001906410.1; XM_001906375.1.
DR   AlphaFoldDB; B2AQD7; -.
DR   GeneID; 6189961; -.
DR   KEGG; pan:PODANSg3439; -.
DR   VEuPathDB; FungiDB:PODANS_4_4490; -.
DR   HOGENOM; CLU_035052_1_0_1; -.
DR   OrthoDB; 4940213at2759; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF47; ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01220)-RELATED; 1.
DR   Pfam; PF00026; Asp; 2.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..412
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002775307"
FT   DOMAIN          79..407
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        95
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   412 AA;  45004 MW;  0CB7DE0D50B0B798 CRC64;
     MKSSLLAFLA VGVAHSAGRL LHATRHGLVP DTVTSNVIPM RKHIVPSSEH RSSVVKPVYR
     RTADVNHPAN LTNVHDVYYI VDIVVGNQTL AVSVDTGSSD TWFVSDYFEC VRFWWQGPEY
     KPNCGLADGF TGNLSGGVLD NPPFVRSYMD TTFVSGYYGF EDVTVGSITA KNQRVGVVNY
     TFWAGDGLTS ALRSPGRVGT RARPDGEVRT PEGSYLALGG LPPVEVDEES WARTKIHGVD
     AIPEWMFEQS DLGLYIIKPD SWVYGRETED VTPAEADQGA VTTHGLTTNT TQFPVLIDVG
     ATLSLLPKGL VQKLYAAFDP PAKYLSTNGL FFALCNATIP KFGVNIGENT FYFAPEDLLR
     QTARDPSGEY CRIGVTDVNG GPYVLGVSFL SSVVAVFDIE NTEMRFASRT KY
//
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