ID A0A0A2VDW8_BEABA Unreviewed; 240 AA.
AC A0A0A2VDW8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE SubName: Full=Pepsin A-3 {ECO:0000313|EMBL:KGQ04280.1};
GN ORFNames=BBAD15_g10526 {ECO:0000313|EMBL:KGQ04280.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ04280.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ04280.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ04280.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ04280.1}.
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DR EMBL; ANFO01001106; KGQ04280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VDW8; -.
DR HOGENOM; CLU_1156194_0_0_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
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 SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..240
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001995462"
FT DOMAIN 64..240
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 240 AA; 26434 MW; B7685C90CE1D1125 CRC64;
MHFYRAGLPL LGVLSLSAQA APQSEDLTAQ RPGIIQMSLK APELSTKSKR QADIDLTYAS
NRKYDIEFSL GTPGQKIVGT FDTGSLYIWV REKAEASVNT NVTRGRSYFN KESSSTLKYT
GESKTAGYGG VANSSFQMDL YRDSLDIKNA NFGIIKNAPK TLDDFNSIFG FGMPDKPSSE
EKGQFVPTMT LLADQGLIGR RLFSLEIGDS GVLIGGVNRK KFWGRLGKQK MTVHPYHGKR
//