ID A0A0N4UV42_ENTVE Unreviewed; 407 AA.
AC A0A0N4UV42;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Peptidase A1 domain-containing protein {ECO:0000313|WBParaSite:EVEC_0000129301-mRNA-1};
GN ORFNames=EVEC_LOCUS1001 {ECO:0000313|EMBL:VDD85858.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000129301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000129301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD85858.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; UXUI01007157; VDD85858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4UV42; -.
DR STRING; 51028.A0A0N4UV42; -.
DR WBParaSite; EVEC_0000129301-mRNA-1; EVEC_0000129301-mRNA-1; EVEC_0000129301.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; 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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
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:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000274131};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..407
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033230044"
FT DOMAIN 89..398
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 107
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 286
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 120..127
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 277..281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 320..357
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 407 AA; 45519 MW; 3AD00EEA723D6D11 CRC64;
MRTLIFLVFF CFIAGNLYAD PVLRIPLKKQ KTIREQLVET NSWHEYVHRR RHLLKKYFHN
LANNELYLLK GKSANEIDEV LRNYMDAQYF GDISIGTPPQ NFTVIFDTGS SNLWVPSKSC
PFYDVACLLH HKYDSSKSST YKSDGRKMQI QYGTGSMKGY ISSDTVCLAD VCAKEQLFAE
ATSEPGLTFI AAKFDGILGM AFPEISVLNI TPVFHTMIEQ KVVAEPNPQD SIGGEITFGG
VDPKRYEEPI TYIPLTRRGY WQFTMDKVLG NGAALGCQKT CQAIADTGTS LIAGPKDQIE
RIQNYIGAEP LFKGEYMVPC DKVPSMPDVT FVIGGKEYSL KSTDYVLNMT AMGKTICLSG
FMGLDLPTRV GELWILGDVF IGRFYTVFDV GKERVGFAQA KPSSENV
//
