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Database: UniProt
Entry: A0A016SPU6_9BILA
LinkDB: A0A016SPU6_9BILA
Original site: A0A016SPU6_9BILA 
ID   A0A016SPU6_9BILA        Unreviewed;       420 AA.
AC   A0A016SPU6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   Name=Acey_s0195.g1494 {ECO:0000313|EMBL:EYB92349.1};
GN   ORFNames=Y032_0195g1494 {ECO:0000313|EMBL:EYB92349.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB92349.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYB92349.1}.
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DR   EMBL; JARK01001531; EYB92349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016SPU6; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT   DOMAIN          97..413
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        337..373
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   420 AA;  46890 MW;  2DC51B52F4FA6946 CRC64;
     MPCSAVQFPP RPKKQRLRSD LHQSDMWISL LLATVLSTAC AQNMTMKLVG TGSLIAKFMK
     ANRYDDYLRL IDEQERSRSN GRYWTWQSLA SWYDEYYLGE VNVGTPAQKF YLSMDTGSSA
     MWLIDGACTH PICNGYATSG RTKNKFYYGK STTFEKTSEK FSINYGTGWA GGFIGVDDIT
     YGTYVVKQQF GVANSLGPFF GTAPMDGIFG LGFNEYENLN APMPTVKHFM DKQQFTVWMN
     RRVAISKGAV GGYITYGAYD KTNCAAKIYY APLAVENKWI INIAGFGIGK YTHTADQHAI
     SDTGTTWIGV PNAVLNNILW QTKSSWDASR KLYTIPCSKM YKLPNMVFHI AGVQFTVPSA
     QYVLDLNLGK GQCVMAIFAV DSAAFGAQFI LGQPFIRTFC QTYDIENQRI GISIATPQKT
//
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