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Database: UniProt
Entry: A0A016SGX9_9BILA
LinkDB: A0A016SGX9_9BILA
Original site: A0A016SGX9_9BILA 
ID   A0A016SGX9_9BILA        Unreviewed;       407 AA.
AC   A0A016SGX9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN   Name=Acey_s0230.g2977 {ECO:0000313|EMBL:EYB89591.1};
GN   ORFNames=Y032_0230g2977 {ECO:0000313|EMBL:EYB89591.1};
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:EYB89591.1, 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   -!- 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:EYB89591.1}.
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DR   EMBL; JARK01001566; EYB89591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016SGX9; -.
DR   STRING; 53326.A0A016SGX9; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24260; -; 1.
DR   PANTHER; PTHR24260:SF136; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..407
FT                   /note="Peptidase S1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001486375"
FT   DOMAIN          50..299
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   407 AA;  46135 MW;  BC36D7B9D2462485 CRC64;
     MLRFFLFFLL FALLFVNSRK LTTEENERNS KKCGVHFLGN EEQNRRSKRS YGGRKFKENE
     YPWTVLLKGQ GECSGVLISQ RHVLTAAHCV LLYDDDHRAE QCNSDKNYNV VAVKISPRSV
     FIHFRATETD CDDAEYCPPH DVAKITVHNL EICTLHNDIA LIELKENISE TVATPICMPS
     EDLQLESVLY AAGSGMDHDA PITLADSSRS SRGQQVVAQR KHSFNKTTKK IVTVTFGKTI
     LPGDSGGPLF QVDESDRHIL VGINSAGNTA RPKANVGQNF EAFHADVRSY LDWICKHSGV
     CPIEDRRADA LPYIRLKKKN VNFKKNTISS LYSIETRRHP ILFERGSSAK YKRRRTLPME
     VLEAQFGDTG KGGVRRYHGV KWLDQCEWIL SAELPQLLVR FESCDVI
//
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