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Database: UniProt
Entry: R0I5E1_9BRAS
LinkDB: R0I5E1_9BRAS
Original site: R0I5E1_9BRAS 
ID   R0I5E1_9BRAS            Unreviewed;       434 AA.
AC   R0I5E1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=CARUB_v10011636mg {ECO:0000313|EMBL:EOA37484.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA37484.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; KB870805; EOA37484.1; -; Genomic_DNA.
DR   RefSeq; XP_006304586.1; XM_006304524.1.
DR   AlphaFoldDB; R0I5E1; -.
DR   STRING; 81985.R0I5E1; -.
DR   GeneID; 17896677; -.
DR   KEGG; crb:17896677; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   OrthoDB; 1213461at2759; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05489; xylanase_inhibitor_I_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR032799; TAXi_C.
DR   InterPro; IPR032861; TAXi_N.
DR   InterPro; IPR033868; Xylanase_inhibitor_I-like.
DR   PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR   PANTHER; PTHR47965:SF22; EUKARYOTIC ASPARTYL PROTEASE FAMILY PROTEIN; 1.
DR   Pfam; PF14541; TAXi_C; 1.
DR   Pfam; PF14543; TAXi_N; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..434
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004343363"
FT   DOMAIN          46..415
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   434 AA;  45820 MW;  8E8FFA13DD63F36C CRC64;
     MASSSPVILS VLVLFIFSLS SSSAQTSFRP KALILPVTKD PSSLQYTTVL NQRTPLVPAS
     VVFDLGGRDL WVDCDRGYVS STYQSPRCNS AVCTRAGSTS CGQCFSPPRP GCSNNTCGAT
     PDNTVTGTAT SGELALDVVS IQSTDGSNPG PVVKIPNLIF VCGSTFLLNG LAKGTVGMAG
     MGRHNIGLPS QFAAAFSFNR KFAVCLTSGR GVAFFGNGPY VFLPGIPISG LQTTPLLISP
     VSTASAFSQG EKSSEYFIGV TAIKIVENTV PINPRLLKIN STGFGGTKIS TVNPYTVMES
     SIYKAFTSEF VRQAAARNIT RVASVKPFGA CFSTQNIGVT RVGYAVPEIQ LVLHSKDVVW
     RIFGANSMVS VRDDVICLGF VDGGVNARTS VVIGGFQLED NLVEFDLASN RFGFSSTLLG
     RRTNCANFNF TSTA
//
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