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Database: UniProt
Entry: A0A0G2EAP0_9PEZI
LinkDB: A0A0G2EAP0_9PEZI
Original site: A0A0G2EAP0_9PEZI 
ID   A0A0G2EAP0_9PEZI        Unreviewed;       400 AA.
AC   A0A0G2EAP0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 32.
DE   SubName: Full=Putative aspartic endopeptidase pep2 {ECO:0000313|EMBL:KKY20047.1};
GN   ORFNames=UCDDS831_g05037 {ECO:0000313|EMBL:KKY20047.1};
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:KKY20047.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY20047.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY20047.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY20047.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY20047.1};
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, ECO:0000256|RuleBase:RU000454}.
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:KKY20047.1}.
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DR   EMBL; LAQI01000106; KKY20047.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2EAP0; -.
DR   Proteomes; UP000034182; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454}.
FT   DOMAIN          87..397
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        118..123
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        323..356
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   400 AA;  43289 MW;  52CD3F42D72665A4 CRC64;
     MKGSMLLAAG AMLGSAQAGV HKMKLKKVPL AEQLEHANIG DHVKALSQKY MGSRPQLNTV
     EDIFRTQPVD ADSEHPVPVT NFLNAQYFSE ISLGTPPQTF KVVLDTGSSN LWVPSSECGS
     IACYLHTKYD SSSSSTYSKN GSSFEIRYGS GSLSGFVSND VFTIGDLTVK DQDFAEATSE
     PGLAFAFGRF DGIMGLGYDT ISVNHIVPPF YNMIEQGLLD DPVFAFYLSD TNDEGAESVA
     TFGGIDESHY SGKLTKIPLR RKAYWEVDLD SITFGDATAD LDNTGAILDT GTSLIALPST
     LAELLNKEIG AKKSFNGQYT VECDKRDGLP DLTFTLTGHN FTITSYDYIL EVQGSCISAF
     MGMDFPEPTG PLAILGDAFL RKWYSVYDLG ENAVGLAKSK
//
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