ID   A0A0C2G193_9BILA        Unreviewed;       449 AA.
AC   A0A0C2G193;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KIH54715.1};
GN   ORFNames=ANCDUO_15138 {ECO:0000313|EMBL:KIH54715.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH54715.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH54715.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH54715.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) 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; KN738612; KIH54715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2G193; -.
DR   Proteomes; UP000054047; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF5; ASPARTIC PROTEASE 10; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 2.
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:0000313|EMBL:KIH54715.1};
KW   Protease {ECO:0000313|EMBL:KIH54715.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..449
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002165652"
FT   DOMAIN          74..445
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        338
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        105..147
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        373..405
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   449 AA;  48715 MW;  5792BA8A8C7DE647 CRC64;
     MINSLILFAV LAMCTLVSSK VHKIDLQYKP SLKMRLYQEG KLEQYLKDKA ALTNKGSALD
     ASSTPVIDYD DMAYMAQITL GTPPQQFVVF LDSGSSNLWV PDVSCAAGQS DTCGTYCKQT
     PYETCLTFCQ PKCCKGSGNT LEVKNACTAK HSFNQTLSST YEKQPGSFQM SYQTGDVSGF
     FGQDTFCVGI LTLALFPEVA FPNSGHFQLY NTTLCATGQI FGQVTTMADG FDKQPEDGML
     GLGWPALAVN GITPPMFNLL NQGELDMPYF VVYMRHLGMH SDLSGGQLTV GGLDTEHCSA
     TYDKIPLTSK TFWQFKMSSV SAGSYSAAPS SGWQVISDTA STFIGGPKTI VDNIAKTVNA
     KWRESLGSYF IECGGNDPDI SFGINGNTYT MTQKNYKISM GAGVCMFAFF PSTAGGFYPS
     WMLGPPLIRE YCQIHDMQGG TIGMAKVIS
//