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Database: UniProt
Entry: A0A0D8XE66_DICVI
LinkDB: A0A0D8XE66_DICVI
Original site: A0A0D8XE66_DICVI 
ID   A0A0D8XE66_DICVI        Unreviewed;       400 AA.
AC   A0A0D8XE66;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   22-FEB-2023, entry version 34.
DE   SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KJH42057.1};
GN   ORFNames=DICVIV_11956 {ECO:0000313|EMBL:KJH42057.1};
OS   Dictyocaulus viviparus (Bovine lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Dictyocaulidae; Dictyocaulinae; Dictyocaulus.
OX   NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH42057.1, ECO:0000313|Proteomes:UP000053766};
RN   [1] {ECO:0000313|EMBL:KJH42057.1, ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH42057.1,
RC   ECO:0000313|Proteomes:UP000053766};
RA   Mitreva M.;
RT   "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX   PubMed=26856411; DOI=10.1038/srep20316;
RA   McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA   Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA   Sternberg P.W., Gasser R.B., Mitreva M.;
RT   "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT   lungworm biology and support future intervention.";
RL   Sci. Rep. 6:20316-20316(2016).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KN716716; KJH42057.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D8XE66; -.
DR   STRING; 29172.A0A0D8XE66; -.
DR   Proteomes; UP000053766; 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; 2.60.40.1960; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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; NAPSIN-A; 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, ECO:0000313|EMBL:KJH42057.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053766};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..400
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002335758"
FT   DOMAIN          97..400
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        128..135
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   400 AA;  46108 MW;  621F8DBE06009479 CRC64;
     MLRPLILLAV CTITFSFLYH EKFHHNPLRK NVVSVPLLRQ STLREKLFEV GSWNIYERKR
     THYQKKLLAK YSSNNIVKLQ FASEIDELLR NYMDAQYFGT IQIGTPPQNF TVIFDTGSSN
     LWIPSRKCPF YDIACMLHHR YDSSASSTYK ADGRKMAIQY GTGSMKGFIS KDNVCMATIC
     AERQPFAEAT SEPGLTFIAA KFDGILGMAF PEISVLGITP VFQTLIDQKK VPSPVFSFWL
     NRNPNSELGG EITLGGMDSR RYMDPITWTR VTRRGYWQFK MDTYMIPCDK VPNLPDISFV
     IENKKFTLEG KDYVLNVRKT DWMLECNDCW KIHLPFWFHG YGFSGKIGEL WILGDVFIGR
     YYTVFDMGQT RLGFAQAKDE NGRPVPPAVL EFKPFEVSKY
//
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