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Database: UniProt
Entry: A0A0B2UZD5_TOXCA
LinkDB: A0A0B2UZD5_TOXCA
Original site: A0A0B2UZD5_TOXCA 
ID   A0A0B2UZD5_TOXCA        Unreviewed;       434 AA.
AC   A0A0B2UZD5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   08-NOV-2023, entry version 34.
DE   SubName: Full=Aspartic protease 6 {ECO:0000313|EMBL:KHN74210.1};
GN   Name=asp-6 {ECO:0000313|EMBL:KHN74210.1};
GN   ORFNames=Tcan_18096 {ECO:0000313|EMBL:KHN74210.1};
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:KHN74210.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN74210.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN74210.1};
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, ECO:0000256|RuleBase:RU000454}.
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:KHN74210.1}.
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DR   EMBL; JPKZ01002949; KHN74210.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2UZD5; -.
DR   STRING; 6265.A0A0B2UZD5; -.
DR   OMA; ACASECT; -.
DR   Proteomes; UP000031036; 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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF45; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KHN74210.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..434
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002077781"
FT   DOMAIN          73..429
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        322
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        104..150
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        357..389
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   434 AA;  48254 MW;  5E5283CD301D8D27 CRC64;
     MTRLFALLLT LTVCSSALVH RIGLTRIESK RTKMIRSGMW EEYVREREVR RTLYNIMEKR
     TSQIVNDYDD MEYLGNITIG TPQQEFLVVL DTGSANLWVP DSSCDRAQPS RCSADCASYK
     WMCRFLCPQE CCTGYEMNAA QFARAASPVC APKNKFDSSK STTYQLDGRK WHLQYGSGSS
     SGFLGIDTVR FGGIGTDQLV VPYTTFGQAT VMDKTFSHSP IDGILGLAFP SLAVENVLPP
     LNNAIRQGLL DEPIFTVWLE HRGAQKGVFG GVFTYGAFDT EHCGGVIAHE PLSSATYWQF
     RMRSIGAAHY ESTGFGYQVI SDTGTSFIGG PKSITDSIAN ALGAKFDYTN QLYLIKCDGH
     LDNIRISIGD HKYEIRPRNY IVELGNGQCA LGMFPMGGAG WGPQWILGDP FIREFCQVHD
     FEKQRIGFAP SKQP
//
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