ID A0A0N4TV88_BRUPA Unreviewed; 392 AA.
AC A0A0N4TV88;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 08-NOV-2023, entry version 35.
DE SubName: Full=Peptidase A1 domain-containing protein {ECO:0000313|WBParaSite:BPAG_0001278201-mRNA-1};
GN ORFNames=BPAG_LOCUS12710 {ECO:0000313|EMBL:VDN93896.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001278201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0001278201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN93896.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; UZAD01013314; VDN93896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4TV88; -.
DR STRING; 6280.A0A0N4TV88; -.
DR WBParaSite; BPAG_0001278201-mRNA-1; BPAG_0001278201-mRNA-1; BPAG_0001278201.
DR Proteomes; UP000038020; Unplaced.
DR Proteomes; UP000278627; 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; 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; 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|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000278627};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..392
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033231385"
FT DOMAIN 69..389
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 89
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 278
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 102..107
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 392 AA; 43706 MW; 17592054D5037B34 CRC64;
MKVLIITAVL ICIVAAVHRT QLTKIESKRK KLFKKGLWSK HLKKKNHFRA TRSRTKIGER
VYDYDDMEYV ANISLGSPIG QQTFLVVLDT GSSNVWIPEV NCVADDCLKK NRFNSSLSKT
YQEDGRTWSI LYGDGSNAQG LLGKDYFAFG PTMKDSLVIP NITFGMARKL SGFKDDPVDG
IVGLAFASIA VDGVTPPLIA AINQSIMKLP LFTVWLDRRG AKENVFGGVF SYGAIDDLNC
DKVIDYEPLS SATFWQFRLR GVKAGQYSIT GTWEAISDTG TSLIAGPKSV INQLGAAVKA
KVYFLYNQNE EMFFLKCDSK SPPVTLIIGS HEYNIQPENY IVMVENNTCI FSFFPMEGNG
FGPTWIFGDP FIRQYCQIYD IGNERIGFAL AK
//