ID A0A016S2E5_9BILA Unreviewed; 416 AA.
AC A0A016S2E5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=Acey_s0309.g2066 {ECO:0000313|EMBL:EYB84820.1};
GN ORFNames=Y032_0309g2066 {ECO:0000313|EMBL:EYB84820.1};
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:EYB84820.1, 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:EYB84820.1}.
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DR EMBL; JARK01001645; EYB84820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016S2E5; -.
DR STRING; 53326.A0A016S2E5; -.
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; 3.
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:SF45; ASPARTIC PROTEASE 6; 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; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..416
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001485970"
FT DOMAIN 72..411
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 90
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 303
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 103..139
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 416 AA; 46726 MW; 31062624F55C1751 CRC64;
MRAIFTLLAL FGCTLPAVHK MTLRRVTPQM MKMLRNGTWS KYVEEFRRYQ QKTPQLNKDR
IYVQEIVSYT EYVGEITIGT PGQTFRVLVD TGTSELWLPD KSCYSHPECQ SSQCDSGLVC
EVFCADQSCC SSQPDKNPCR RKRLFDSQKS STYENVEGRF ELQRKRYAEG FYGQDTLRIG
AAGTDQLVIE QVLLGQAEKI GASLAYANFD GVLGISFTGV SPILTAVLDD LLEKPIVTVF
YKRVGNKEDV YGGMVTYGGQ DVENCEASVT YEEVNWPVLW QIKLRKVSAG KYSSNAGWQA
ESDTGTSFIR GPAPIISDIA KELGAEYDQS KDLYFIDCDA PATITFEIGA KKYTVNSENL
IIEVEGKLCV LALSHLPHYG DKNEPKWTLG SPFIREYCHI YDIDAHKIGF AKAYQN
//
