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Database: UniProt
Entry: A0A0K0DFA0_ANGCA
LinkDB: A0A0K0DFA0_ANGCA
Original site: A0A0K0DFA0_ANGCA 
ID   A0A0K0DFA0_ANGCA        Unreviewed;       339 AA.
AC   A0A0K0DFA0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peptidase A1 domain-containing protein {ECO:0000313|WBParaSite:ACAC_0000962601-mRNA-1};
OS   Angiostrongylus cantonensis (Rat lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000962601-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000035642}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:ACAC_0000962601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   AlphaFoldDB; A0A0K0DFA0; -.
DR   STRING; 6313.A0A0K0DFA0; -.
DR   WBParaSite; ACAC_0000962601-mRNA-1; ACAC_0000962601-mRNA-1; ACAC_0000962601.
DR   Proteomes; UP000035642; 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   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF45; ASPARTIC PROTEASE 6; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035642}.
FT   DOMAIN          36..336
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   339 AA;  36950 MW;  09B639A0E7D61FAA CRC64;
     MRHTFTMNCF YRNSNESGCK KNILIRDNGD VMNHEFVGNI TLGTPDQQFA VMLDTGSADL
     WVPGKNCKAE NGTSTLISFS GSGSGKQEFD SGSSSTFVGG NRTWAIKYGL GEVKGVRGTD
     VMKVGNAATY VCFSDSKTIL LQDCSDGVLG LGFTSLSVDH TVPPLINAID QSLLDKPLFT
     VWILGLRGLF TYGAIDTEKC GKIIAYEPLS SETYYQFKVC YQAMYEAASD TGTTFIGGPR
     VIVDELAKAA GAVYNATEDL YLIECNAILP TLDITIGTKK YRIDSIYYVL KKGNTCFLAI
     ISSEFGAFGP NWVLGIPFIR QYCNIFDIGQ KRIGFALSL
//
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