ID R0F7F1_9BRAS Unreviewed; 360 AA.
AC R0F7F1;
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_v10006223mg {ECO:0000313|EMBL:EOA17822.1};
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:EOA17822.1, 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; KB870811; EOA17822.1; -; Genomic_DNA.
DR RefSeq; XP_006284924.1; XM_006284862.1.
DR AlphaFoldDB; R0F7F1; -.
DR STRING; 81985.R0F7F1; -.
DR MEROPS; A01.A33; -.
DR GeneID; 17878773; -.
DR KEGG; crb:17878773; -.
DR eggNOG; KOG1339; Eukaryota.
DR OrthoDB; 640027at2759; -.
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 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121}.
FT DOMAIN 56..357
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 74
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 258
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 249..253
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 284..318
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 360 AA; 39585 MW; 648F796922921140 CRC64;
MMNSLKLKRL LIAPVYLSLL LQSLAVQGII RVGLTMNYSS FDINGVRLSN INDNIYIGEI
KVGTPSQRFK VVFDTGSINL WVPSTKSMGS KHNLYVSSKS SSYKPIGRNV TLEYGTGSLR
GILSSDTINV GGITITNQCF TEALATRTGD DPLLKAPFDG ILGLGNPQDS ATRTLSVWES
IKTQGRVEKK IFSIWLGRPS LFKAEGEITF GGIDRSRFKG QHIYVTATGE KYFFQMNNIL
VGSQDTSVCS RGCQVFVDSG NSNIHGPAAL IKEINRRIGA APNCSNVKRL PDVTFTIGGS
SFSVSSRDYI YRVTKNKCTS RFVETNDIYW TLGMPFMRAV HTVYDFTTEP TVKIGFAKSA
//
