ID   CARP_PODAS              Reviewed;         425 AA.
AC   O13340;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Podosporapepsin;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=PAPA;
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9524217; DOI=10.1016/s0378-1119(98)00057-2;
RA   Paoletti M., Clave C., Begueret J.;
RT   "Characterization of a gene from the filamentous fungus Podospora anserina
RT   encoding an aspartyl protease induced upon carbon starvation.";
RL   Gene 210:45-52(1998).
CC   -!- INDUCTION: Expressed under carbon starvation conditions.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; AF016054; AAC49997.1; -; Genomic_DNA.
DR   PIR; JC6557; JC6557.
DR   AlphaFoldDB; O13340; -.
DR   SMR; O13340; -.
DR   MEROPS; A01.044; -.
DR   VEuPathDB; FungiDB:PODANS_6_11460; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06097; Aspergillopepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease; Cleavage on pair of basic residues; Disulfide bond;
KW   Glycoprotein; Hydrolase; Protease; Signal; Zymogen.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..91
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025877"
FT   CHAIN           92..425
FT                   /note="Podosporapepsin"
FT                   /id="PRO_0000025878"
FT   DOMAIN          108..419
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        310
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        346..381
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   425 AA;  45921 MW;  DA66CAA215183214 CRC64;
     MVSLTDLFLA SLLVPTSPWL CLPPRIDTID QRGGRVTLKQ VRNPRGHKAF NPARATYRTF
     LKYGVPAPDY IKKAVAHIDE EQEEAFARIK RDTGSAAAIP INEVDIAYVT PVTIGTPPQT
     LMLDLDTGSS DLWVFSSLTP SNQVRGQEIY SPTKSSTSKL LSGHTWSIRY GDGSGSRGTV
     YTDNFTIGGL EVKSQAVQAA LEVSSMLTQE QSLDGLVGLG FSALNTVRPS SQLTFFDNAR
     PNLDEEVFTA DLKYHATGSY DFGFIDSKKY AGNITYTAVQ QSPGYWTHSL SGYSVGSGAF
     QASQISGISD TGTTLLYLPT AIVTAYYRQV QGAQNSQYYG GYVFPCSSTL PTFTFGIEGA
     RFTIPASYIN YTRISPTSTT CYGGLQSSSG LGINIFGDVA LKRAFVVFSG TNPPRIGFAI
     KPLAS