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Database: UniProt
Entry: A0A166ZAA7_9HYPO
LinkDB: A0A166ZAA7_9HYPO
Original site: A0A166ZAA7_9HYPO 
ID   A0A166ZAA7_9HYPO        Unreviewed;       395 AA.
AC   A0A166ZAA7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   SubName: Full=Vacuolar protease A {ECO:0000313|EMBL:OAA37714.1};
GN   ORFNames=BBO_07422 {ECO:0000313|EMBL:OAA37714.1};
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:OAA37714.1, ECO:0000313|Proteomes:UP000076863};
RN   [1] {ECO:0000313|EMBL:OAA37714.1, ECO:0000313|Proteomes:UP000076863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA37714.1,
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:OAA37714.1}.
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DR   EMBL; AZHA01000029; OAA37714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166ZAA7; -.
DR   OrthoDB; 615305at2759; -.
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   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:OAA37714.1}.
FT   DOMAIN          85..392
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        284
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        116..121
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   395 AA;  42391 MW;  21F3F46C103F7503 CRC64;
     MKSALIAAAA LAGSAQAGIH KMKLQKIPLA EQLVGASFEA QAHQLGQKYL GARPASRADI
     MFNNQVAESK DGHPVPVTNF ANAQYFSEIT IGTPPQTFKV VLDTGSSNLW VPSQSCNSIA
     CFLHSTYDSS SSSTYKKNGS DFEIRYGSGS LSGFVSNDKV SIGDLTIKNT DFAEATSEPG
     LAFAFGRFDG ILGLGYDTIS VNKIVPPFYQ MINQKLLDEP VFAFYLGSED SGSEAIFGGV
     DKDHYEGKIE YIPLRRKAYW EVDFDAIAFG DEVAELENTG VVLDTGTSLN TLPTDLAELL
     NKEIGAKKGF GGQYTIDCKA RDSLPDITFT LAGSNYTLPA SDYILELGGS CVSTFTPLDM
     PEPVGPLAIL GDAFLRRYYS VYDLGKGAVG LAKAK
//
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