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
//