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Database: UniProt
Entry: A0A0C2GLC9_9BILA
LinkDB: A0A0C2GLC9_9BILA
Original site: A0A0C2GLC9_9BILA 
ID   A0A0C2GLC9_9BILA        Unreviewed;       322 AA.
AC   A0A0C2GLC9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   08-NOV-2023, entry version 32.
DE   SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KIH59764.1};
GN   ORFNames=ANCDUO_09995 {ECO:0000313|EMBL:KIH59764.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH59764.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH59764.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH59764.1,
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; KN731626; KIH59764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2GLC9; -.
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; 2.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KIH59764.1};
KW   Protease {ECO:0000313|EMBL:KIH59764.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..322
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002149197"
FT   DOMAIN          69..156
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   322 AA;  36759 MW;  A2C333C4E335A1BA CRC64;
     MKAAWVFLSM LHVGFTLNFT MEVYDWGSLA KNLIATGNYT EYLEKLDKIR YSNLEWKWQG
     LNDYFDQFYL GVVTVGTPHQ VFYLHMDTGS SNMWVIDQAC RQRQCTGYPA GYRPKLKFKP
     GASSTFRKIP QGFHMKYYTG SADGYYGTDT ITFAGFFQFF TTTMSYGAMV GYIQYGALDT
     THCITAINWV PLSLPKYWQF PIQGFQIGNF VWNSVDQVIT DSGASFIGTP MAVFNGILRA
     TNAKYMPAHR MHVVPCAKMW AQPNLIFRIS GHQYVIPSHQ YVIDMKLGHG YKLAFSEVVT
     NPHHTLIHNT IEKQNIAETS CD
//
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