GenomeNet

Database: UniProt
Entry: A0A167IIE9_9HYPO
LinkDB: A0A167IIE9_9HYPO
Original site: A0A167IIE9_9HYPO 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system