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
//