ID R0F8R8_9BRAS Unreviewed; 326 AA.
AC R0F8R8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=CARUB_v10006868mg {ECO:0000313|EMBL:EOA18347.1};
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:EOA18347.1, 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, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KB870811; EOA18347.1; -; Genomic_DNA.
DR RefSeq; XP_006285449.1; XM_006285387.1.
DR AlphaFoldDB; R0F8R8; -.
DR STRING; 81985.R0F8R8; -.
DR MEROPS; A01.A33; -.
DR eggNOG; KOG1339; Eukaryota.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF91; EUKARYOTIC ASPARTYL PROTEASE FAMILY PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121}.
FT DOMAIN 21..323
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 226
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 252..283
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 326 AA; 36210 MW; C89DDBC7A975E8DE CRC64;
MGNTSFNKHG VELENSYDNI YYGDITIGTP GQRFTVVFDT GSSDLWVPSG DKWEADEPHN
LYDSQKSSTY KPNGTNVALG YATGDLKGIL SSDTVDIGGI TITDQYFTEA RSTPEKDPLR
EAPFDGILGL GSPQISATET RPVWYSMMRQ GKIEEKMFSI WYGRSEDSGA GGEIVFGGKN
TAHYTGEHFY VNVREDDDYF FFQMNNIFFG TIDTNICSTG CKVFVDSGST SIVGPSGSIA
DIKERIGAKL DCKNLEKLPD VTFTIEGRSF SVSPHDYIRL SDCTTRFVGS DNYDFWILGM
PFIRAFHTVF DFEKLPTVRV GFAKSV
//
