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Database: UniProt
Entry: A0A0C2H1F7_9BILA
LinkDB: A0A0C2H1F7_9BILA
Original site: A0A0C2H1F7_9BILA 
ID   A0A0C2H1F7_9BILA        Unreviewed;       398 AA.
AC   A0A0C2H1F7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   08-NOV-2023, entry version 33.
DE   SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KIH65359.1};
GN   ORFNames=ANCDUO_04321 {ECO:0000313|EMBL:KIH65359.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH65359.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH65359.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH65359.1,
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; KN727590; KIH65359.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2H1F7; -.
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: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; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000313|EMBL:KIH65359.1};
KW   Protease {ECO:0000313|EMBL:KIH65359.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..398
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002149477"
FT   DOMAIN          74..391
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        315..351
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   398 AA;  44879 MW;  1E022C4FDF002BA4 CRC64;
     MWITLVLANT FLLSAVRALN MTVELHGTGS LIAKFIKANR YDYYLRVLEE QERNRTKGRY
     WTWQALASWY DEFYLGEVKV GTPPQKFLLA MDTGSSAMWL IDGACTHPIC NGYPNSGRTK
     NKFYYGESIT FKRTSDHFSL NYGSGWAGGF TGADDISYGT FIVKQQQFGV ANSLGPFFGT
     APMDGIFGLG FNEYPNLNAP MPTVKHFMDK EQFTVWMNRR VAISRGAIGG YITYGQYDKT
     NCEPQIYYAP LAVDNKWIIN IAGFSIGSFT HTANQHAISD TGTTWIGVPN AVLNNILWQT
     QSWWDPNRKL YIIPCSKMWT LPRMIFHIAG RKFTVPSVQY VLDLNLGNGQ CVMAMFAVDS
     AAFGAQFILG QPFIRTFCQT YDMANKRIGI SVARPQKT
//
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