ID A0A016TSD9_9BILA Unreviewed; 440 AA.
AC A0A016TSD9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=Acey_s0080.g1322 {ECO:0000313|EMBL:EYC05700.1};
GN ORFNames=Y032_0080g1322 {ECO:0000313|EMBL:EYC05700.1};
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:EYC05700.1, 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:EYC05700.1}.
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DR EMBL; JARK01001416; EYC05700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016TSD9; -.
DR STRING; 53326.A0A016TSD9; -.
DR MEROPS; A01.A76; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF5; ASPARTIC PROTEASE 10; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..435
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 103
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 328
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 116..159
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 440 AA; 50140 MW; C5AA3FC96BD4A05A CRC64;
MLITLEGAMY ISTFIILTII WCAAATVYQV PLVKMEFKRD QMMRTGEWAA HVQRRNAEWS
DLNAKTHSDK RFRQQDVTNY YDEEYLANIS IGTPAQKFQM LLDLKSPYFW VPDYTCAPPV
RPKGCEYDTC WTGMACLVFC PKKNHCCFGR RHKRDTYPCR GRKTYDPRDS ETIVETDEDF
DALFGEFEAS GIYSIETVIF GDDRMKHLVA EGIKFGRAKR AYGFHESAMD GVFGLGFVDP
HEEDYVPALL QAAELGLVKP IFTIYLKHVG AQVDVHGGVL TLGGIDDVHC DKDVVYVKLA
AQSLWSFFIS GISIKNFSYN KVMHAESDTK DPFIICPAEI ADAIAKEVGA QYNDTDDVYY
IDCSAKPVVE LRIENNKFTI GSVNLVRKTS DSRCILNFRG VVLPSVFEMV WNFGHPFMRE
YCHIFDVDNQ RIGFAKSLQK
//
