ID A0A016VAA2_9BILA Unreviewed; 652 AA.
AC A0A016VAA2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=Acey_s0014.g2378 {ECO:0000313|EMBL:EYC24206.1};
GN ORFNames=Y032_0014g2378 {ECO:0000313|EMBL:EYC24206.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC24206.1, 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:EYC24206.1}.
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DR EMBL; JARK01001350; EYC24206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016VAA2; -.
DR STRING; 53326.A0A016VAA2; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
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; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
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..652
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001489143"
FT DOMAIN 283..613
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 652 AA; 69363 MW; 96D2AF68A09FE877 CRC64;
MLPFIILLVF SPISWAGVNR KSGNHPYGNY DFPPEAYAPS SSGKQADPVS SVDKILEEGL
GPEIVPQKVE MGPGPVIPEK HVMEMGPGPV IPHQLPMEPG PVIPEKNRVE MGPGPVIPSR
QPSMGPGPVI PPHHLSMGAG PVIPPHYVPL EPGPVIPEEH IVPMEPGRML RPVNPFHHPS
MGPGPELLPL PFMEEPGPVI SPRSSPTNPY QEEPEMGPGP VIPQPIPEGP GPVVLPQGPG
PVIVPPHMQM GPGPVIPQPV PEGPGPVILP PQHIQQGPGP VIVPPHMQMG PGPVITQPIP
EGPGPVILPP QHFQQGPGPA IVPPSMQMGP GPVIPQPIPG GPGPAIPSHP IQQGPGPVMV
PPHLQMGPGP VIFSQRAPRD LSPFMAGPEI PFLPEDSPFM SREDPTDGIL GLAFTSLAVD
RVVPPLINAI NQNLLDQPLF TVWMEHRGKL EGAVGGVFTY GAVDTKNCGP VTAYEPLSSA
TYYQFKMAAI GMGSYTNSKV YQVISDTGTS FIGGPKTVTD ALAKAAGAKY SAFQESYTIP
CNAKPPTLDV TIGSHKYSID PVNYIVSAGT NQCLFAIFPF EFGGFGPSWI LGDPFIRQFC
NIYDIGQKRM GFAPSLQNSN TDDERYDRDH ESFAGSTPFI LLLLLPLAFL ME
//