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Database: UniProt
Entry: A0A158PPI9_ANISI
LinkDB: A0A158PPI9_ANISI
Original site: A0A158PPI9_ANISI 
ID   A0A158PPI9_ANISI        Unreviewed;       411 AA.
AC   A0A158PPI9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   08-NOV-2023, entry version 30.
DE   SubName: Full=Peptidase A1 domain-containing protein {ECO:0000313|WBParaSite:ASIM_0001479201-mRNA-1};
GN   ORFNames=ASIM_LOCUS14202 {ECO:0000313|EMBL:VDK51745.1};
OS   Anisakis simplex (Herring worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC   Anisakis simplex complex.
OX   NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001479201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ASIM_0001479201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK51745.1, ECO:0000313|Proteomes:UP000267096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; UYRR01031657; VDK51745.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158PPI9; -.
DR   WBParaSite; ASIM_0001479201-mRNA-1; ASIM_0001479201-mRNA-1; ASIM_0001479201.
DR   Proteomes; UP000036680; Unplaced.
DR   Proteomes; UP000267096; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF44; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267096};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..411
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035044864"
FT   DOMAIN          55..403
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        86..123
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   411 AA;  45664 MW;  191A1785DE4A213F CRC64;
     MLRSELSLLV LVAFGFVFWY VDAAVHQMPL MKQTSQRVKM MREGRWVYRY TDFEFFGVIT
     IGTPEQKFLV ALDTSSSILW VPDSTCGTPL CDSSKEWSSQ CMLDQSNVII CNTIELWQSS
     EVCKIKQNFN SSASETYESV GGNWTIQNGI IDAAGLFGKD VVRFGKKGGS QLVVANTTFG
     QASAISDSFE YYEAGGILGL GFQSTAFGEV LPPLNNAWDQ RLLDKRVFTV WLHPMNSGIN
     YGPAGIFTYG GVDSHNCEGN VVYQPLSSDA HWQFTMKSIS FGTYRSNATS YEVLSDTGSS
     YIEGPFVMIN SIAKKLGATY DPTYDLFFSN CSGFTKNIKI EIGDHTYEIE PTNYILQGTE
     GICMLMLHPI DGMGLGPQVF LGTPFIRQYC HIYDVDNKQI GFSKAKIPVS D
//
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