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Database: UniProt
Entry: A0A162KGG8_9HYPO
LinkDB: A0A162KGG8_9HYPO
Original site: A0A162KGG8_9HYPO 
ID   A0A162KGG8_9HYPO        Unreviewed;       388 AA.
AC   A0A162KGG8;
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 aspartic {ECO:0000313|EMBL:OAA50794.1};
GN   ORFNames=BBO_00741 {ECO:0000313|EMBL:OAA50794.1};
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:OAA50794.1, ECO:0000313|Proteomes:UP000076863};
RN   [1] {ECO:0000313|EMBL:OAA50794.1, ECO:0000313|Proteomes:UP000076863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA50794.1,
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:OAA50794.1}.
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DR   EMBL; AZHA01000002; OAA50794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162KGG8; -.
DR   OrthoDB; 656651at2759; -.
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:SF51; NAPSIN-A; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..388
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007836545"
FT   DOMAIN          77..385
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   388 AA;  40069 MW;  F2EA14FC304FD440 CRC64;
     MRYTSLSILV AAEAILASPV ERATKPSVVP VKHVVNVSSP SGLVAKGQAR INKVNGAEKT
     LGNIDASGPA ENDDVSYVAS VAIGSASWDL IVDTGSSNTW TGAQKSYVPY STGNDTGGTV
     AVSYGSGQFS GEEYVDKVTF AGLTVKSQSI GSASNAVGFN GVDGIFGLGP VGLTQNTVSN
     AATVPTFLDN LYKQGSIPSE VLGVYFKPEA GSDTNDNNGE LTLGGVDSTK YTGTLNYVPT
     LKSGTAAAYW GVSIASFNYG STVLASGSTG IVDTGTTLIY IPSAAYSKYL SASGGRTDTS
     TGLVSYTTKP TGNFSIKIGT ITYTLTPAQY LIPTSQYGFF GLSSSKYYSW IANGGTGSVN
     TIIGQKFLEN YYSVYDTTNA RIGFATAA
//
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