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
//