ID A0A158R213_NIPBR Unreviewed; 376 AA.
AC A0A158R213;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE SubName: Full=Aspartic protease 3 (inferred by orthology to a C. elegans protein) {ECO:0000313|WBParaSite:NBR_0001480701-mRNA-1};
GN ORFNames=NBR_LOCUS14808 {ECO:0000313|EMBL:VDL78402.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Trichostrongyloidea; Heligmonellidae; Nippostrongylinae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0001480701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0001480701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL78402.1, ECO:0000313|Proteomes:UP000271162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; UYSL01021502; VDL78402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158R213; -.
DR STRING; 27835.A0A158R213; -.
DR WBParaSite; NBR_0001480701-mRNA-1; NBR_0001480701-mRNA-1; NBR_0001480701.
DR OMA; IACRMHN; -.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; 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; 2.40.70.10; 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; 2.
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:UP000271162}.
FT DOMAIN 48..370
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 66
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 258
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 79..86
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 292..329
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 376 AA; 40973 MW; C1BED824A2ADFB82 CRC64;
MYKTSYPRSA YKAKSIAEYL KQKYIKGYKF DSNLAYEEGL SDYSNAQYYG PIQIGTPPQT
FQVLFDTGSS NLWVPSKTCK ASDIACDFHQ KFDCKKSSTC TATGAPFEIQ YGSGSMKGVV
DNDIVCFGKD HTWCTDKTQG FAAATQEPGV AFVAAKFDGV LGMGWDRISV NNIPQPMDQI
FANKALCAEP VFAFWLSRDA NNVANGGEMT LCGTDPAHYK GSIAWEPLVS EDYWRIKLSN
VAIQGTSYTN GPVDAIVDTG TSLLTGPTDE IKKIQKKIGA IPLLGGEYEM ECSRIPNLPP
ITFTLGGQDF VLQGSDYILQ ITQNGQTQCI SGFMGLDIPA PAGPLWILGD VFIGKFYSVF
DNGNKRVGFA QSAISN
//