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Database: UniProt
Entry: A0A0A2W0M4_BEABA
LinkDB: A0A0A2W0M4_BEABA
Original site: A0A0A2W0M4_BEABA 
ID   A0A0A2W0M4_BEABA        Unreviewed;       451 AA.
AC   A0A0A2W0M4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Podosporapepsin {ECO:0000313|EMBL:KGQ12000.1};
GN   ORFNames=BBAD15_g2254 {ECO:0000313|EMBL:KGQ12000.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ12000.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ12000.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ12000.1,
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:KGQ12000.1}.
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DR   EMBL; ANFO01000154; KGQ12000.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2W0M4; -.
DR   STRING; 1245745.A0A0A2W0M4; -.
DR   MEROPS; A01.081; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_606887_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   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..451
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001996254"
FT   DOMAIN          71..444
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   451 AA;  51241 MW;  B1C7971B65E2B018 CRC64;
     MRSTALIGIV TTISSVFAVN PISPGCDEEF ADDVGMGIDK RSDLINAVPN FFKQNGTFAL
     RFHKSPFGHR FTVPVQIGDP PEFLELDVHI GMATTWVLGP DPVTRGGWPV ADRKVWVPGN
     SSEHVKRKKG FKNFDLWYPE KHAVQGTVYR DRMSIGEGSQ AFGYWHQDFG VAKEIHPRFV
     SENSFVGVLG LGYKSDRGAH LPESIVTNMQ ENLGHSWRFS IAFKESGGMY KFSSKMIQEL
     TSVGHMDWNM HDDSRHTGDL FRTVYYNNDK IPDGNQNSYH VLNMTGYAFG SGKIRKKIFQ
     AGMDSTTSYI LAPQPIAEDY YRTIGAPTRE IKLPTGHRGW EVPCKKKLPD FVIEFTNTTT
     RIGNELLDGE KKYWGFRKYN ISGESLVLQK TRADPKRKKE WCLGAIVQNE DKFYPDRAGL
     AVSEEQMDSV WQVPRHHNRR SFLRNGHGSR Y
//
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