GenomeNet

Database: UniProt
Entry: A0A090LKE9_STRRB
LinkDB: A0A090LKE9_STRRB
Original site: A0A090LKE9_STRRB 
ID   A0A090LKE9_STRRB        Unreviewed;       387 AA.
AC   A0A090LKE9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Aspartic peptidase family and Aspartic peptidase domain-containing protein {ECO:0000313|EMBL:CEF70267.1, ECO:0000313|WBParaSite:SRAE_2000490000.1};
GN   ORFNames=SRAE_2000490000 {ECO:0000313|EMBL:CEF70267.1,
GN   ECO:0000313|WBParaSite:SRAE_2000490000.1,
GN   ECO:0000313|WormBase:SRAE_2000490000};
OS   Strongyloides ratti (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF70267.1};
RN   [1] {ECO:0000313|EMBL:CEF70267.1, ECO:0000313|Proteomes:UP000035682}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC   ECO:0000313|WBParaSite:SRAE_2000490000.1}, and ED321 Heterogonic
RC   {ECO:0000313|EMBL:CEF70267.1};
RA   Martin A.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SRAE_2000490000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; LN609529; CEF70267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090LKE9; -.
DR   STRING; 34506.A0A090LKE9; -.
DR   MEROPS; A01.053; -.
DR   EnsemblMetazoa; SRAE_2000490000.1; SRAE_2000490000.1; WBGene00265147.
DR   WBParaSite; SRAE_2000490000.1; SRAE_2000490000.1; WBGene00265147.
DR   WormBase; SRAE_2000490000; SRP01187; WBGene00265147; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   OMA; PWRSKHY; -.
DR   OrthoDB; 2874784at2759; -.
DR   Proteomes; UP000035682; Chromosome X.
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; 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:UP000035682};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..387
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015030924"
FT   DOMAIN          73..384
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        312..346
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   387 AA;  43165 MW;  B74BFBC3746E8A0C CRC64;
     MKLFLTFFTF ISITLAVVFE HQLFKVESKR KRLIRQGKWK EYMKQKNFMR HNFKNQVLAS
     VSESVNDYDD VEYLGNISIG TPSQYFSVLF DTGSSNLWIP GNACEECLEK HQFNPSESKT
     YIRTGKMFNI NYGYASVSGI LGQDTVAFVG NNGKLSIPNT IFGRAHNISW LFKDDILDGI
     LGLAFPSISI DGILPPMFNA QKQGLLNKPI FTAYLQHIQP ANGELGGSLT FGDIDTKNCG
     PVIAYEKLYS STYWAFKLNK ISLGSFNISK VFNAISDTAI GILGLPQYLV DGIAKTIGAK
     FNDEYKIYTV KCSQTFPDLN LTIGQHTYSI KSNKLVVDMD LGDNLCMVGM FSVSGMGIQV
     ILGNSFIQSY CNIYDFGNNQ IGFAIPK
//
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