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
//