ID A0A0A2VLK4_BEABA Unreviewed; 399 AA.
AC A0A0A2VLK4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Pepsin A {ECO:0000313|EMBL:KGQ08776.1};
GN ORFNames=BBAD15_g5877 {ECO:0000313|EMBL:KGQ08776.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ08776.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ08776.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ08776.1,
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:KGQ08776.1}.
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DR EMBL; ANFO01000542; KGQ08776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VLK4; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_1_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; 2.
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:SF89; SACCHAROPEPSIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..399
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002006982"
FT DOMAIN 68..395
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 86
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 279
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 399 AA; 43161 MW; 09143B50376E3EF3 CRC64;
MKIPSSVAVV SLLSLVHLVQ SAITLPLKPL DKKIGSMIKQ YTKTKAGEPG KITVPVKDWI
KHTADLQWYT EIEVGSPPQK FNVIFDTGSF DMFIANKNCT SAGNSRLFDS DKSSTFNQQP
NQPSGFGYGT GVDSIPLQYN GEGVSGVIVT DKVGIAGHAV DHQQFLLCDQ YPEFMADVPF
DGVMGIGVEG ATDMPSGKAW YWALYASGQL DSPEFSLYYP AGKVDGAEMT LGGTNPSRYK
GDIHKVKLNR DANFVVDQPS LTINGKPLAA AANQKTILDS GTAYFAAPSK IVSAFYKAVS
PKIKQLNHEA WGVECDIIES LAVEITFTFG SGAETFNATM PRESFNLGPY EGKPGICQTV
FSSIDALGGK FLIGGPLLKQ YYTVWDGHNM EMGFAELKN
//
