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Database: UniProt
Entry: A0A016U5R4_9BILA
LinkDB: A0A016U5R4_9BILA
Original site: A0A016U5R4_9BILA 
ID   A0A016U5R4_9BILA        Unreviewed;       409 AA.
AC   A0A016U5R4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   08-NOV-2023, entry version 35.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   Name=Acey_s0056.g2661 {ECO:0000313|EMBL:EYC10286.1};
GN   ORFNames=Y032_0056g2661 {ECO:0000313|EMBL:EYC10286.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC10286.1, 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:EYC10286.1}.
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DR   EMBL; JARK01001392; EYC10286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016U5R4; -.
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; 4.
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}.
FT   DOMAIN          56..405
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        87..127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   409 AA;  45329 MW;  63142BFFBEAA444A CRC64;
     MPLTKIDSPM IRMMREGIWR DMMKKRNAAR LKMRTSARTF IDERQQDVFN YHDVEYIGNI
     TIGTPEQSFQ VVLDTGSADF WVSDVSCIPP PRTEGCENSF CDPGLVCKIF CPYKDLCCNA
     IPRKYTCIGK HVYDPAKSRS FFERPGTWSI KYRSGSASGI YGHDMVGFGG AGMQNRLEVP
     DVVVGRATQL SKIFKDVPFD GVLGLAFQAI ATNDAVMPPF VHAHELNLVE PIFTVHLRRV
     GGSDDGFGGV FTYGGVDTQN CAGNIMYEPL TEAGYWQFKM RSVSIGGFRS SLGWQVVSST
     GSAFIGAPKS VADAIALAVN AELRPEEDAY FLDCDGFPTL KFGIGRNVYQ VEGYNFMITL
     AEYKCILALY GMDGGSFGPS WILGAPFIRQ YCTIHDMQNK RIGFANSLE
//
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