ID   A0A0G2H394_9PEZI        Unreviewed;       396 AA.
AC   A0A0G2H394;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 26.
DE   SubName: Full=Putative aspartic endopeptidase pep1 {ECO:0000313|EMBL:KKY23245.1};
GN   ORFNames=UCDDS831_g02976 {ECO:0000313|EMBL:KKY23245.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY23245.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY23245.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY23245.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY23245.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY23245.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKY23245.1}.
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DR   EMBL; LAQI01000068; KKY23245.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2H394; -.
DR   Proteomes; UP000034182; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06097; Aspergillopepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF2; ASPERGILLOPEPSIN-1-RELATED; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
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..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..396
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002544702"
FT   DOMAIN          76..388
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   396 AA;  41649 MW;  22C93E208C665CD7 CRC64;
     MSSVIFFPAL FAMVAFAAPQ VVGPLNQTFT IPQVPHAQVL KNGPLAVQRT YLKYGVPVPD
     FVSEAVANSA ADAAGLSERS VAATPADGFD TLYLSPVTLG WVFSTLMASG STNGQSLYNP
     SRSGVLLPQQ SWTITYGDSS GGSGLVYADK VVVGEVTATK QSVEAATSAS SLFVQDTNSD
     GVMGLAFSNL NSVRPTPQRT FFDTVKNTLA KPLFTALLKK GAAGKYDFGF LDTTSYTGSI
     VYTNVLTTPK PGFWGFNATG YSIGSGAVVQ KSISSIIDTG TSLFYLPSDV VAAYYARVPG
     ASKSTYFGGW IVPCTSTPPA FSTVISGSLV TMPGSYLIYG AVDQSNNCYG GIQENTGIGF
     SIYGLIFLKS QYIVFDQTSA NAPRLGFARQ QGVSYV
//