ID   A0A0N4X2P0_HAEPC        Unreviewed;       436 AA.
AC   A0A0N4X2P0;
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:HPLM_0001863001-mRNA-1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001863001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0001863001-mRNA-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0N4X2P0; -.
DR   WBParaSite; HPLM_0001863001-mRNA-1; HPLM_0001863001-mRNA-1; HPLM_0001863001.
DR   OMA; ISESYWS; -.
DR   Proteomes; UP000038042; 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; 2.
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:SF40; ASPARTIC PROTEASE 3; 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}.
FT   DOMAIN          123..433
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        330
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        154..161
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        360..394
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   436 AA;  49601 MW;  76B20E3DF71B4BAE CRC64;
     MVSFPLLLLS TCLSFEEMIR VKDPVPLKKT TIRRRRSSFI ENLAGDYRRM VYFPEYGIHT
     RYVHFTKQGH IHVNVFEPEY WNNLHNGYKP EYGNNLNNDY NMGNWNSLHG SSEILYNYLD
     MQYYGPIQIG HPPQIFTVVF DTGSSNLWVP CANCLGTADF CRSHSKFNYK ESFTCIRKHR
     PLNLTYGIGS AKGSLYSDIV CIDTNPKHCF RQEFVCAQRV HEMDGTIPDG TLGMAWPSLS
     VDNITTPLEH LFANKMDCPK AVFAFWLNRN SIEGGELTIC GTDPSRYQDP IIWVPLISES
     YWSVLLGGIT VKAESGDILH IPGNFSASID SGTSFIVGPS EKIQKILDFI GVMELEVIEC
     SAVPSYPTIF FKLGSYEFKL EGQQYTLKQS HGECYVAFQK NPSKDDNSWT LGDAFMSNFY
     TIFDYENKKV GFAKPA
//