ID A0A0G2EMD9_9PEZI Unreviewed; 494 AA.
AC A0A0G2EMD9;
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 pep1 {ECO:0000313|EMBL:KKY23499.1};
GN ORFNames=UCDDS831_g02919 {ECO:0000313|EMBL:KKY23499.1};
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:KKY23499.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY23499.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY23499.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY23499.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY23499.1};
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:KKY23499.1}.
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DR EMBL; LAQI01000066; KKY23499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2EMD9; -.
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: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; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..494
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002543663"
FT DOMAIN 86..389
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 473..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 102
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 284
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 494 AA; 51016 MW; E3F34513D52AA232 CRC64;
MPSFRTVAAC AAILSLATAT PIEKRSKTFT CEQVKRGSVA RNGPAQMLKA FNKFGGVAPS
EVVSAAAAGK TGSAAAVPED EIDTLYLTPV TVGDTTLQLD MDTGSSDLWV FSTLLSDSNQ
SNHSVYDPTV SGTKQDGSSW NITYGDGSGA AGTVYADKVV VGGVTATSQA VEAATSISSS
FVEDTDTDGI LGLAFGSLNT VKPEAQVPFF DTVANDLAEK LFAVTLKRGE AGSYDFGFRN
ESKYTGDIAY VDVDTSNGFW EFAPSGYAVG NGSVVNASID AIADTGTSLL LLPEAIVTAY
YDTIEGSAYF AQFGGFVFPC GDVPDFTLVI GGQERTVPGE YINYSAIFGP LCYGGIQVDT
GIGYSIIGDI FLKVSSLKTS TNLKTSATPT LLFRSNGKNL GASPTTRSLG GLATVIGVSV
VNSTSSPATG ALSIFPTATP VVAATSIRSC VLATNGTLSP NRFLAHSCHA QSRGPSTVGV
PQCMQTKPHA SPSL
//