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
//