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Database: UniProt
Entry: A0A0C2FPR0_9BILA
LinkDB: A0A0C2FPR0_9BILA
Original site: A0A0C2FPR0_9BILA 
ID   A0A0C2FPR0_9BILA        Unreviewed;       194 AA.
AC   A0A0C2FPR0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KIH48694.1};
GN   ORFNames=ANCDUO_21233 {ECO:0000313|EMBL:KIH48694.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH48694.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH48694.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH48694.1,
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; KN757682; KIH48694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2FPR0; -.
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   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
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   Hydrolase {ECO:0000313|EMBL:KIH48694.1};
KW   Protease {ECO:0000313|EMBL:KIH48694.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..194
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002148671"
FT   DOMAIN          1..189
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   194 AA;  21427 MW;  221331993279CB7E CRC64;
     MSMGLLSGVI TFGLIARGHC HPKIYWVPLS WAAYWQFAIE GFQVGGFVSR QHQQVPPGSF
     PIHSFHALSP RSFKAISDTG KSFLGGPPVA ISGIIRESGA RYSPYYRMYV VPCSTMNRHL
     DLIFTINGKS FAVPSGQYII NLDIGGGWCT LAVFPIHAGG FTTQWIMGTP WIRTFCSTYD
     FGNKRIGFSV ARPL
//
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