ID J4WLL3_BEAB2 Unreviewed; 427 AA.
AC J4WLL3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative aspartyl protease {ECO:0000313|EMBL:EJP70625.1};
GN ORFNames=BBA_00255 {ECO:0000313|EMBL:EJP70625.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP70625.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP70625.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP70625.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; JH725150; EJP70625.1; -; Genomic_DNA.
DR RefSeq; XP_008593574.1; XM_008595352.1.
DR AlphaFoldDB; J4WLL3; -.
DR STRING; 655819.J4WLL3; -.
DR GeneID; 19883267; -.
DR HOGENOM; CLU_606887_0_0_1; -.
DR InParanoid; J4WLL3; -.
DR OrthoDB; 335768at2759; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:EJP70625.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..427
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003782560"
FT DOMAIN 71..426
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 427 AA; 48347 MW; 7CFFD1E3F0144489 CRC64;
MRSTALIGIF TTISSVFAVN PASPGCGEEF ADDVGMGIDK RSDLINAVPN FFKQNGTFAL
RFHKSPFGHR FTVPVQIGDP PEFLELDVHI GMATTWVLGP DPVTRGGWPV ADRKVWVPGN
SSEHVKRKKG FKNFDLWYPE KHAVQGTVYR DRMSIGEGSQ AFGYWHQDFG VAKEIHPRFV
SENSFVGVLG LGYKSDRGAH LPESIVTNMQ ENLGHSWRFS IAFKESGGHM DWNMHDDSRH
TGDLFRTVYY NNDKIPDGNQ NSYHVLNMTG YAFGSGKIRK KIFQAGMDST TSYILAPQPI
AEDYYRTIGA PTREIKLPTG HRGWEVPCKK KLPDFAIEFT NTTTRIGNEL LDGEKKYWGF
RKYNISGESL VLQKTRTDPK RKKEWCLGAI VQNEDKFYPD FVLGWPFLKN KWIQFGKFHG
ITIGEAS
//
