ID   PEPA_PHANO              Reviewed;         406 AA.
AC   Q69IF8; Q0V1U6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Aspartic protease SNP2 {ECO:0000305};
DE            EC=3.4.23.-;
DE   AltName: Full=Protease 2;
DE   Flags: Precursor;
GN   Name=SNP2 {ECO:0000303|Ref.1}; ORFNames=SNOG_02018;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bindschedler L.V., Sanchez P., Cooper R.M.;
RT   "Secreted proteases and depolymerases from Stagonospora nodorum during
RT   infection of wheat.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Secreted aspartic endopeptidase that allows assimilation of
CC       proteinaceous substrates. The scissile peptide bond is attacked by a
CC       nucleophilic water molecule activated by two aspartic residues in the
CC       active site. Shows a broad primary substrate specificity. Favors
CC       hydrophobic residues at the P1 and P1' positions.
CC       {ECO:0000250|UniProtKB:Q12567}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q12567}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01103}.
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DR   EMBL; AY135713; AAP30888.1; -; Genomic_DNA.
DR   EMBL; CH445327; EAT90230.1; -; Genomic_DNA.
DR   RefSeq; XP_001792636.1; XM_001792584.1.
DR   AlphaFoldDB; Q69IF8; -.
DR   SMR; Q69IF8; -.
DR   STRING; 13684.SNOT_02018; -.
DR   EnsemblFungi; SNOT_02018; SNOT_02018; SNOG_02018.
DR   GeneID; 5969486; -.
DR   KEGG; pno:SNOG_02018; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_0_1_1; -.
DR   InParanoid; Q69IF8; -.
DR   OMA; YGSGNAK; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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   3: Inferred from homology;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..65
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q12567"
FT                   /id="PRO_0000407059"
FT   CHAIN           66..406
FT                   /note="Aspartic protease SNP2"
FT                   /id="PRO_0000407060"
FT   DOMAIN          92..399
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        325..360
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   406 AA;  42567 MW;  5E8BB15BB90B6CAB CRC64;
     MPSFTYLTAA LALTSSVVAS PVEKRDAFEV KQVAHGLHRK NGPAQIAKTL RKYGKAVPAH
     IQAAADNNAV VQADANTGSD PAVPSDQYDS SYLSPVTVGT STVHLDFDTG SADLWVFSDL
     QAKSSLSGHD YYKTDASKRK SGYTWKISYG DGSGASGQVY TDKVTVGQVT ATAQAVEAAT
     SVSAQFSQDV DTDGLLGLAM SSINTVKPQQ QTTWFDTVKS QLAKPLFAVT LKYHAAGTYD
     FGYIDSAKYT GAITYVNADA SQGFWGFTAS GYSVGTGATV SSSISGILDT GTTLMYVPAA
     TAKAYYAKVS GAKLDSTQGG YVFPCSATLP NFSITVAGVK QTVPGKYINY APITDGSSTC
     FGGMQPDTDI GQSIFGDIFL KSKYIVHDMS NGTPRLGFAQ QAGVSS