ID   A0A0B2VIV5_TOXCA        Unreviewed;       276 AA.
AC   A0A0B2VIV5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Aspartic protease 6 {ECO:0000313|EMBL:KHN80980.1};
DE   Flags: Fragment;
GN   Name=asp-6 {ECO:0000313|EMBL:KHN80980.1};
GN   ORFNames=Tcan_15622 {ECO:0000313|EMBL:KHN80980.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN80980.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN80980.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN80980.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHN80980.1}.
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DR   EMBL; JPKZ01001612; KHN80980.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2VIV5; -.
DR   STRING; 6265.A0A0B2VIV5; -.
DR   OMA; IQENGYC; -.
DR   Proteomes; UP000031036; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF8; ASPARTIC PROTEASE 1-RELATED; 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; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000313|EMBL:KHN80980.1};
KW   Protease {ECO:0000313|EMBL:KHN80980.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036}.
FT   DOMAIN          1..266
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        190..226
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KHN80980.1"
SQ   SEQUENCE   276 AA;  30266 MW;  3E777BE02AB77957 CRC64;
     SKTFTNLTKP FKAIYGSGYS NGYFASDVLN FSNFSIPAQE FGVATSLAPV FGMQPIDGIM
     GLGWPSLTKN NARPPMQNLL GQLDEPIFTV WMDSTPRLSQ GGVGGLITYG GFDSTNCAPD
     VNWIPLSSMS YWQFPIQGFA IGQLSINIEQ QAISDTGTSW IGGPSYYINL ILSQIGAVYN
     PYFRMNTISC IQRFTSPELI FFIGNRRYTI ASSDYIFDVQ LGGGLCGVAL FAMNGKGKIP
     AWSLGDIFIR KYCNVYDIGG KRIGFSLAKH SLRESF
//