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Database: UniProt
Entry: A0A0M3K9P6_ANISI
LinkDB: A0A0M3K9P6_ANISI
Original site: A0A0M3K9P6_ANISI 
ID   A0A0M3K9P6_ANISI        Unreviewed;       546 AA.
AC   A0A0M3K9P6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   08-NOV-2023, entry version 35.
DE   SubName: Full=Peptidase A1 domain-containing protein {ECO:0000313|WBParaSite:ASIM_0001769001-mRNA-1};
GN   ORFNames=ASIM_LOCUS17094 {ECO:0000313|EMBL:VDK59485.1};
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_0001769001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ASIM_0001769001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK59485.1, 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; UYRR01033734; VDK59485.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M3K9P6; -.
DR   WBParaSite; ASIM_0001769001-mRNA-1; ASIM_0001769001-mRNA-1; ASIM_0001769001.
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; 2.
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:SF40; ASPARTIC PROTEASE 3; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 2.
DR   SUPFAM; SSF50630; Acid proteases; 2.
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..546
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035110474"
FT   DOMAIN          77..443
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        117..122
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   546 AA;  60892 MW;  E898C087B13DC8CF CRC64;
     MFSAIQFFIV LLALSCATDA LYRVQLTRRK RILNTEAKRK PSPSRSFRYF ANKFTYPPML
     AEEPYDLPLN NYKNTIYTGT ITIGVPPQEF EASFYHFENK VNFDTGSDLL WVNCAGCSAG
     DCQKRAAFNC SQSRYCSPVD AKPDPIKYAK GHAWGPIDKD YVCVCLKIVV IIEQIFDSAN
     SFLEFLSRSE LAELSIGDAS SGFCGRKRQN LTCAMQRGEL AILEDGIFGL SAEGLQPGTE
     SAMGQLLRYS GCEEKKVAFW LNRDSEAKNG GEVTICGVDK NHYQGDLVWI PLEHGPHWYV
     RMDDVLIGSH RMSLGQTEAV IDSGWSYMAV PSEEYFKVTF NARNSLLCRC SSVDELPTLT
     FVLNGNPFSI PPEAYAVKVL FDTGSWPLWV DCVGCSDEEC QKRAKFSCSQ STTCSLVNVK
     PTFCPYVQGE VSGPLDRDVV CIGNSSNRFC TEVSQNFVCA TKRNGIEMQS VHDKYEFSCD
     GVFGLSAEGE SPEEESAMGQ FLRNSACKEK KVAFWLNRDF GAENGGEVTI CGVDKNHYQV
     IPLREF
//
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