ID   C5MRP0_STEFE            Unreviewed;       402 AA.
AC   C5MRP0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   22-FEB-2023, entry version 47.
DE   SubName: Full=Aspartyl protease-like protein {ECO:0000313|EMBL:ACS32298.1};
OS   Steinernema feltiae (Entomopathogenic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=52066 {ECO:0000313|EMBL:ACS32298.1};
RN   [1] {ECO:0000313|EMBL:ACS32298.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=G26 {ECO:0000313|EMBL:ACS32298.1};
RA   Ma J., Chen S.L.;
RT   "Construction and Analysis of SSH libraries of Steinernema feltiae G26.";
RL   Submitted (MAY-2009) 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; GQ150477; ACS32298.1; -; mRNA.
DR   AlphaFoldDB; C5MRP0; -.
DR   MEROPS; A01.053; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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: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; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:ACS32298.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..402
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002955430"
FT   DOMAIN          76..396
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          40..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        287
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   402 AA;  43009 MW;  E527D887428A2AAC CRC64;
     MFKIVVLAAL AAVLNAAVFQ HEVKSVGSMR AKMIAAGTWK DRLSSSAPRD RSLSSTTTTT
     STSATSPSEP PVSPESPPSS SIPSAQPFTI VLDTGSSNLW VINSNCKTQA CQGYPGAPTK
     HRFDESKSTT FKNDGTFFSI QYGSGSCDGK LGVDTLSVGF PPLAGISFAT QKFGISDEIA
     DVFGYQPVDG ILGLGWPALA EDNVVPPMQN VLNQLDQPLF TVWMDRHVKQ TQGGNGGLIT
     YGAIDTKNCD ATVNYVPLSA TTYWQFVMDG CEIGTYKRAR REQVISDTGT SYIIGPTDVV
     ENIAQVIGAQ LDWENDMYTV NCNAQLPPLV LKIGGQTYSI PSVEYVLDLS LGGGKCGIAI
     QGQDAGGYGP AWILGDTFIR SYCLVYDIGQ KRIGFAKAHH NL
//