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
//