ID J4UNB6_BEAB2 Unreviewed; 443 AA.
AC J4UNB6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 08-NOV-2023, entry version 47.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:EJP66527.1};
GN ORFNames=BBA_04467 {ECO:0000313|EMBL:EJP66527.1};
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:EJP66527.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP66527.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP66527.1,
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, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; JH725159; EJP66527.1; -; Genomic_DNA.
DR RefSeq; XP_008597786.1; XM_008599564.1.
DR AlphaFoldDB; J4UNB6; -.
DR STRING; 655819.J4UNB6; -.
DR MEROPS; A01.081; -.
DR GeneID; 19887479; -.
DR HOGENOM; CLU_035052_0_0_1; -.
DR InParanoid; J4UNB6; -.
DR OrthoDB; 4940213at2759; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF47; ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01220)-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EJP66527.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762}.
FT DOMAIN 100..441
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 118
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 332
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 443 AA; 47634 MW; A2E848737F2680DD CRC64;
MKASILVSAL AVAASGIKEQ RHASDWDLSQ PMNGITFERV KAVTMAKPDR PTPRFSRLKH
VAGKKGNHGT ISALGRALRS TPGSVKQTFQ NISSVGAYST QYAIQCGWDG KPVWLLFDTG
SSDTWAAKSD FDCIDSVGNS HDQAACGFGT SLVDDFGQGT IDELHFLLRY GSGEKISGPM
GYSDLSCGGV TVTKQQVGLA NSTYWRGNNA TVGILGLAYP SITSAYYGEI GDEATWNAIT
YTPFLTNAII QGGLDPVFSV ALSKNSSDGV LAWGGLPPID WVRGDSASTD LIVANLIDQA
ETAWKYSFYT IIPDGVRWGQ TTDATRYPYI VDTGTTLMYL PPPLAEAIAM SFQPRAVYLY
QWGMYFAPCN SIPPSFAITV SGVDLWINPA DMIYHDLVDP LTGYCAIAVA SGGQGPYILG
DAFLQNVVAV FDVGAAQMRF YSR
//
