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
//