ID A0A158PFD7_ANGCS Unreviewed; 373 AA.
AC A0A158PFD7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Peptidase A1 domain-containing protein {ECO:0000313|WBParaSite:ACOC_0000327301-mRNA-1};
GN ORFNames=ACOC_LOCUS3274 {ECO:0000313|EMBL:VDM54859.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000327301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000327301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM54859.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM54859.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-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; UYYA01000928; VDM54859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158PFD7; -.
DR STRING; 334426.A0A158PFD7; -.
DR WBParaSite; ACOC_0000327301-mRNA-1; ACOC_0000327301-mRNA-1; ACOC_0000327301.
DR OMA; IQENGYC; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; 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; 2.
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:SF8; ASPARTIC PROTEASE 1-RELATED; 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 Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..373
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033730723"
FT DOMAIN 69..373
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 270
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 373 AA; 40866 MW; AD1D5C0C2501E9D0 CRC64;
MKTILVLATL AAIAHGKTYT METRSSGSLI SRLMKEKRYQ KYLEERNLHR SQVLVKGSQP
VEDVFDTYYL VNITVGTPGQ NFSLLLDTGS SSLWVIDISC NTKACYSLSP ERRRFNSSTS
STFSTQNRTL FIGYDFGSCN GRIATDTVSF AGICKFLDAE SLSDDFTYMP YDGILGLGWP
AVSVGNITPP MQNLLPALDA PLFTVWLERQ INVSYGGAGG LVTFGAVDTT NCELDVNYVP
LTSEAYGQFP LSGFSIGRFS KKFTQDAVSD TGSSWIGVPP YLINTVAGYT GGQYDTGYQF
YTVNCSTMMT QPDVEFTIND VKYSLKSEDY VIDLGLGGGQ VSASTSTQQF SGPIDWTALV
LYVVRLILQI CTL
//
