ID   C0JAA3_9ORYZ            Unreviewed;       519 AA.
AC   C0JAA3;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   22-FEB-2023, entry version 49.
DE   SubName: Full=Aspartic proteinase nepenthesin-1 {ECO:0000313|EMBL:ACN85284.1};
OS   Oryza australiensis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4532 {ECO:0000313|EMBL:ACN85284.1};
RN   [1] {ECO:0000313|EMBL:ACN85284.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19164767; DOI=10.1073/pnas.0812798106;
RA   Lu F., Ammiraju J.S., Sanyal A., Zhang S., Song R., Chen J., Li G., Sui Y.,
RA   Song X., Cheng Z., de Oliveira A.C., Bennetzen J.L., Jackson S.A.,
RA   Wing R.A., Chen M.;
RT   "Comparative sequence analysis of MONOCULM1-orthologous regions in 14 Oryza
RT   genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:2071-2076(2009).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; FJ032634; ACN85284.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0JAA3; -.
DR   MEROPS; A01.050; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05472; cnd41_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033873; CND41-like.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR032799; TAXi_C.
DR   InterPro; IPR032861; TAXi_N.
DR   PANTHER; PTHR13683:SF750; ASPARTYL PROTEASE AED1; 1.
DR   PANTHER; PTHR13683; ASPARTYL PROTEASES; 1.
DR   Pfam; PF14541; TAXi_C; 1.
DR   Pfam; PF14543; TAXi_N; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           39..519
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002897975"
FT   DOMAIN          180..515
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          55..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        396
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   519 AA;  53540 MW;  BC8C9AC5ACDA8C2F CRC64;
     MAAAASARCA GHGGGGFLLR RRLLAAVTFL AAFGLVAADD AAAGRGRHPH HVMLSVEDMF
     PGPPSSSSCD DAPREHKHGA TSSGTRMTIV HRHGPCSPLA DAHGKPPSHE DILAADQNRA
     ESIQHRVSTT ATGRGNPKRS RRAPSRRQQP SSAPAPAASL SSSTASLPAS SGRALGTGNY
     VVTVGLGTPA SRYTVVFDTG SDTTWVQCQP CVVVCYEQRE KLFDPARSST YANISCAAPA
     CSDLDTRGCS GGNCLYGVQY GDGSYSIGFF AMDTLTLSSY DAVKGFRFGC GERNEGLFGE
     AAGLLGLGRG KTSLPVQTYD KYGGVFAHCL PARSSGTGYL DFGPGSPAAA GARLTTPMLT
     DNGPTFYYVG MTGIRVGGQL LSIPQSVFTT AGTIVDSGTV ITRLPPAAYS SLRSAFASAM
     AARGYKKAPA VSLLDTCYDF TGMSQVAIPT VSLLFQGGAR LDVDASGIMY AASVSQVCLG
     FAANEDGGDV GIVGNTQLKT FGVAYDIGKK VVGFSPGAC
//