ID A0A167IIE9_9HYPO Unreviewed; 443 AA.
AC A0A167IIE9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE SubName: Full=Peptidase A1 {ECO:0000313|EMBL:OAA49126.1};
GN ORFNames=BBO_02171 {ECO:0000313|EMBL:OAA49126.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA49126.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA49126.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA49126.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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:OAA49126.1}.
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DR EMBL; AZHA01000004; OAA49126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167IIE9; -.
DR OrthoDB; 4940213at2759; -.
DR Proteomes; UP000076863; 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}.
FT DOMAIN 98..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; 47909 MW; C2E9473530EE4074 CRC64;
MKASILVSAL AAAASGLKEQ RHASDWDLSQ PMNGITFERV KAVTMAKPDR PTPRFSRLKH
VAGKKGNHGT ISTLGRALRS TPGNVKQTFQ NISSVGAYST QYAIHCGWDG KPVWLLFDTG
SSDTWAAKSD FDCIDSVGNS HDQAACGFGT SMVDDFGQGT IDELHFLLRY GSGEKISGPM
GYSDLSCGGV TVTKQQVGLA NSTYWRGNNA TVGILGLAYP AITSAYYSEI GDEATWNAIT
YTPFLTNAII QGGLDPVFSV ALSKNSSDGV LAWGGLPPID WVRGDSASTD LIVANLIDQA
ETAWKYSFYT IIPDGVRWGQ TTDTTRYPYI VDTGTTLMYL PPPLAEAIAM SFQPRAVYLY
QWGMYFAPCN SIPPRFAITI SDVDFWINPA DMIYHDLVDP LTGYCAIAVA SGGQGPYILG
DAFLQNVVAV FDVGAAQMRF YSR
//