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Database: UniProt
Entry: A0A016VXF0_9BILA
LinkDB: A0A016VXF0_9BILA
Original site: A0A016VXF0_9BILA 
ID   A0A016VXF0_9BILA        Unreviewed;       427 AA.
AC   A0A016VXF0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   Name=Acey_s0003.g1189 {ECO:0000313|EMBL:EYC31697.1};
GN   ORFNames=Y032_0003g1189 {ECO:0000313|EMBL:EYC31697.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC31697.1, 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, ECO:0000256|RuleBase:RU000454}.
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:EYC31697.1}.
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DR   EMBL; JARK01001339; EYC31697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016VXF0; -.
DR   STRING; 53326.A0A016VXF0; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
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; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF45; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..427
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001494023"
FT   DOMAIN          72..422
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        103..143
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   427 AA;  47645 MW;  F16F465C53AA827F CRC64;
     MLLLLVLLAE TNYAVAEAYQ VPLVKIQSEM MRMLRAGTWA AHVKEMRAMR SNVMKAPGTL
     RQDINAYHSM EYVVNITVGT PEQNFTVALD TGTADTWVID ASCAANKPAH CWDSVCDEGL
     VCEVFCPDRA CCEIEAPMGI NPCKGKRYFE SAKSSSYVPV DGRWWMAYRP HRKLAFGFYG
     NDTLRFGGSG TKQLVVPVTK IGFADKIDNY FGKRSLDGIL GMAFPFLSYN DVVSPFEQAW
     KLGLVEPIFT VYMERVGWEA ENVYGGAVTY GGLDTQHCGD VIAYQPLTTA YPTFWQIEVD
     NFTTGGFVYE YPASAISDTS SSFFGVNSFF VEEIASNMSA TYSKDHDLYF IDCDANPSIT
     ISIGKRLYEI ESKNLIIHVE GDTCILAIYH YSFIGGTWVL GAPFIRQFCT IYDMANKQIG
     FAKSLQK
//
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