ID   A0A0N5A6H8_PARTI        Unreviewed;       422 AA.
AC   A0A0N5A6H8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peptidase A1 domain-containing protein {ECO:0000313|WBParaSite:PTRK_0001760100.1};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001760100.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001760100.1}
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; A0A0N5A6H8; -.
DR   STRING; 131310.A0A0N5A6H8; -.
DR   WBParaSite; PTRK_0001760100.1; PTRK_0001760100.1; PTRK_0001760100.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; Acid Proteases; 4.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..422
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005892745"
FT   DOMAIN          68..416
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        86
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        99..137
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   422 AA;  46499 MW;  E7C23633ADFFF272 CRC64;
     MKFIIITFAI ISLLEAITFK HSLYRVESVR KRLMKTGEWP LYLKRKEFYL SNLKTTKQTV
     KDYEDMEFLA NITIGTPPQT FVIVPDTGSS NLWIPDSTCG SSVKQCPSYC EDSVICQFLC
     DPSCCKSNEK SSRQSNCDQK NKFNSAKSST YVENGQPFTI QYGSGNAEGF LGTDTVRFVG
     DYGTLDVPRT TFGQATTISN DFTNSPADGI LGLAFKSIAV DGITPPIINA INQNLLDQAI
     FTVYLQHKGL ESTYGTPGGA FTYGAFDSDN CNSQIDYYKL QSATYWQFVI NGISIGSTNI
     RRSFSVISDT GTSLIAGPPA VVERITTIVG ATYNQNYGAY LIKCDASFPD VALSINGKNY
     KILSKYLVDQ IGNGMCMFGI FGMNMGGYGP QWILGDPFIM SYCQVYDIGN RRIGFALPKS
     TN
//