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Database: UniProt
Entry: A0A0G2ENP2_9PEZI
LinkDB: A0A0G2ENP2_9PEZI
Original site: A0A0G2ENP2_9PEZI 
ID   A0A0G2ENP2_9PEZI        Unreviewed;       410 AA.
AC   A0A0G2ENP2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   SubName: Full=Putative aspartyl protease {ECO:0000313|EMBL:KKY23736.1};
GN   ORFNames=UCDDS831_g02767 {ECO:0000313|EMBL:KKY23736.1};
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:KKY23736.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY23736.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY23736.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY23736.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY23736.1};
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:KKY23736.1}.
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DR   EMBL; LAQI01000064; KKY23736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2ENP2; -.
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   CDD; cd06097; Aspergillopepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 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:SF23; ASPARTIC ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15950)-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; 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, ECO:0000313|EMBL:KKY23736.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..410
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002543675"
FT   DOMAIN          98..407
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        335..370
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   410 AA;  43348 MW;  30B4119C63D96DB5 CRC64;
     MHSFRVAILL VALLAAVVLA RPAPTKTTQT LAKRSFKVPR NLNPKIKRKD GAAAMRRAMR
     KFGIKHQAAA AAAATPASNA TNENGEVAAN PEENEALFLS PVKIGGQTMN MDFDTGSSDL
     WVFSTQLSKQ AIGGHAAFDS AKSKSFQAMD GASFLITYGD GSGAAGNVGL DTVDIGGATV
     TKQAIEMATA VSQSFQQDTN TDGLVGLAFS KINTVKPQKQ KTFFDNIMKD LDQPVFTADL
     TNDTSGTYEF GTIDKSKFKG ELTYTAVDNS QGFWQFPSKS FMVDGQKMTN TKGSDAIADT
     GTSLLMVDDN VAKAYYAKVK GAVNDPQAGG FVYPCDAVMP DIAVAVGDYM ANIPGDQVTF
     APVDEANTTC FGGVQGNQGS DLQIFGDTMF KAQFVAFNGG NQSLGMAPKN
//
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