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Database: UniProt
Entry: A0A183KT17_9TREM
LinkDB: A0A183KT17_9TREM
Original site: A0A183KT17_9TREM 
ID   A0A183KT17_9TREM        Unreviewed;       225 AA.
AC   A0A183KT17;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Peptidase A1 domain-containing protein {ECO:0000313|WBParaSite:SCUD_0001820901-mRNA-1};
GN   ORFNames=SCUD_LOCUS18206 {ECO:0000313|EMBL:VDP65123.1};
OS   Schistosoma curassoni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0001820901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SCUD_0001820901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP65123.1, ECO:0000313|Proteomes:UP000279833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dakar {ECO:0000313|EMBL:VDP65123.1}, and Dakar, Senegal
RC   {ECO:0000313|Proteomes:UP000279833};
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}.
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DR   EMBL; UZAK01040748; VDP65123.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183KT17; -.
DR   STRING; 6186.A0A183KT17; -.
DR   WBParaSite; SCUD_0001820901-mRNA-1; SCUD_0001820901-mRNA-1; SCUD_0001820901.
DR   Proteomes; UP000050789; Unplaced.
DR   Proteomes; UP000279833; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.60.40.1960; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF51; 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; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279833}.
FT   DOMAIN          1..214
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        138..175
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   225 AA;  26170 MW;  47CFC02778ABB368 CRC64;
     MSKYGNIPVF PNILQNFPNM DPIFSFYLSH GNDMNDNKMD LLLRCRENGT SFGGEMVLGG
     VNPEYFEGDL EYMPTVNNNI WAVRMSSLMI NDTEFCNGCT AFIDTGTSTI IGGREQVTRI
     NTMLGISYQF GRRNFLDCKR IDMLPPIEFI FRKKKYTLEP QDYVIKEDFW FKTVCSSPFD
     IDDSVPPNFW ILGDVFMRRF YTVFDFGQKR IGLTYVLNKK NETRI
//
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