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Database: UniProt
Entry: A0A0B1SSU7_OESDE
LinkDB: A0A0B1SSU7_OESDE
Original site: A0A0B1SSU7_OESDE 
ID   A0A0B1SSU7_OESDE        Unreviewed;       268 AA.
AC   A0A0B1SSU7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   08-NOV-2023, entry version 33.
DE   SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KHJ86577.1};
DE   Flags: Fragment;
GN   ORFNames=OESDEN_13665 {ECO:0000313|EMBL:KHJ86577.1};
OS   Oesophagostomum dentatum (Nodular worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Strongyloidea; Chabertiidae; Oesophagostominae; Oesophagostomum.
OX   NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ86577.1, ECO:0000313|Proteomes:UP000053660};
RN   [1] {ECO:0000313|EMBL:KHJ86577.1, ECO:0000313|Proteomes:UP000053660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ86577.1,
RC   ECO:0000313|Proteomes:UP000053660};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Oesophagostomum dentatum.";
RL   Submitted (MAR-2014) 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; KN559952; KHJ86577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B1SSU7; -.
DR   Proteomes; UP000053660; 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   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF8; ASPARTIC PROTEASE 1-RELATED; 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   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KHJ86577.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053660};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..268
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002064953"
FT   DOMAIN          72..268
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   NON_TER         268
FT                   /evidence="ECO:0000313|EMBL:KHJ86577.1"
SQ   SEQUENCE   268 AA;  29354 MW;  E930B9CA549074CA CRC64;
     MRTLRVVLLV GTLVAMAHPK SFKMRTRSGG SLRARLIASG KYAPYLEKQR IRALQILSKG
     SQPFLDYADD FYLGEVQVGT PGQNITLVLD TGSSNMWVID EACKSPECNG KPESSYPKNK
     FKTDASKTFK KGSRTFSLTY GSGSCNGYLA TDTVSFAGIT VPKQEFGVAT KIAEVFGYQP
     VDGILGLGWP ELATEKVVPP MQNILSQLDK PIFTVWLDRK VKPSKGGSGG LITYGDMDTE
     NCAPDVNYVK LSSLTYWQFP MEGFSLGR
//
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