ID A0A0N4VUE5_HAEPC Unreviewed; 259 AA.
AC A0A0N4VUE5;
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_0000091201-mRNA-1};
GN ORFNames=HPLM_LOCUS913 {ECO:0000313|EMBL:VDO06977.1};
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_0000091201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0000091201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO06977.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO06977.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; UZAF01000946; VDO06977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4VUE5; -.
DR STRING; 6290.A0A0N4VUE5; -.
DR WBParaSite; HPLM_0000091201-mRNA-1; HPLM_0000091201-mRNA-1; HPLM_0000091201.
DR OMA; MAYISNI; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; 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 Gene3D; 2.60.40.1960; -; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000268014}.
FT DOMAIN 1..259
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DISULFID 196..230
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 259 AA; 27952 MW; 176237A5716CEB74 CRC64;
FNCSQSSTCT QTYQYVPIQY GTGSTQGYVD NDVVCFGTNH QYCTNNQQGF LCAMQEPGET
FVDKPFDGIL GMAWDSIAQG GVAQPMTQIF ANQAICPEAV FAFWLNRDLF NNVIGGELTL
CGIDPTHYQG TIAWEPLISE TYWQIQLGGL TVNGQQIIDG PVGAIVDSGT SLIAGPPALV
QEIQQAIGAE YESIDCSTIP SLPPITFTIG GTELTLTAKQ YVIQYTDGTC GSGFQEFQNP
VPGVSWILGD VFIGTFYSI
//