ID A0A0B2W556_TOXCA Unreviewed; 399 AA.
AC A0A0B2W556;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 08-NOV-2023, entry version 31.
DE SubName: Full=Aspartic protease 6 {ECO:0000313|EMBL:KHN88410.1};
GN Name=asp-6 {ECO:0000313|EMBL:KHN88410.1};
GN ORFNames=Tcan_07400 {ECO:0000313|EMBL:KHN88410.1};
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:KHN88410.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN88410.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN88410.1};
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:KHN88410.1}.
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DR EMBL; JPKZ01000233; KHN88410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2W556; -.
DR STRING; 6265.A0A0B2W556; -.
DR OMA; DEEYIGN; -.
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:SF44; 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:KHN88410.1};
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..399
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002077945"
FT DOMAIN 77..394
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 109..114
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 320..354
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 399 AA; 44142 MW; 1A6DEFD6FF7D00C6 CRC64;
MKLFLIQLAF VTLTAAVVTR VPLLHIETRR IRLIREGKWE EHRRMKEELR SIRIKAGSSK
PRVVSSQGVN DYDDLEYVGN ITIGTPPTQQ FNVVLDTGSS NLWIPDSTCT TSDCSLKHRY
NANASSTHSI DGRQWRVIYG DGSNANGYLG TDVITLGGVG EAQLRIQSQT FGQATSMMGF
RNDPVDGILG LGFTALADDF VEPPVINAIA QKLLDEPIFT VWMQAAGYQQ NVYGGQFTYG
GLDPEHCGPV IAYQPLSMAS FWQYRMKAIG VGNYLNRKGW EVIADTGTSF IGGPAYVIDE
IGAALGAKYD HYNQLYFVPC GSEDTLINIV LYVGEHKYEI EPRNYIVKMT TNKCAVGMFG
YSSGGYGPTW ILGDPLIRQY CVIHDVGQQR IGFARSKTA
//