ID R0FJ97_9BRAS Unreviewed; 391 AA.
AC R0FJ97;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=CARUB_v10003127mg {ECO:0000313|EMBL:EOA22472.1};
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:EOA22472.1, 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; KB870810; EOA22472.1; -; Genomic_DNA.
DR RefSeq; XP_006289574.1; XM_006289512.1.
DR AlphaFoldDB; R0FJ97; -.
DR STRING; 81985.R0FJ97; -.
DR GeneID; 17883388; -.
DR KEGG; crb:17883388; -.
DR eggNOG; KOG1339; Eukaryota.
DR OrthoDB; 663919at2759; -.
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 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 PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR PANTHER; PTHR47965:SF68; 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|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..391
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004350032"
FT DOMAIN 43..373
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 391 AA; 42195 MW; 0341075525A51076 CRC64;
MAPRVIFVFL SLVFLYLANT SHSLEKIQSF LHPINKDEAT NLYSIPLNIG SGFSKEYVLD
LNGVSPLLQN CATAAKSSSF HPIRCGSTRC TYANPSFSCP KNTTTKAKTP CRSSDNARLF
RDTVPLLYTF NGVYIMDSEK SSSLTLTCTD GAPVKGTIGL ANTHLSIPSQ LISMYHLAPK
MALCLPNSKD KSTINYPGGL WIGKGEYYYL PYLKDVSKIF ASTPLIGNAK SGEYLIDVKS
IQVGGKNVPI LHGATKISTL APYTVLQTSI YKALLTAYAV NANMAKAPAV KPFGACFSSS
GGRGAPMMDL VLRGGAKWRI HGANSLVKVN KNLVCLGFVD GGVNPKNPIV IGGFQMEDNL
VEFDLKASIF SFSSSLLLHN TSCSVERLSP F
//
