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
//