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
//