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
//