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Database: UniProt
Entry: R0IC05_9BRAS
LinkDB: R0IC05_9BRAS
Original site: R0IC05_9BRAS 
ID   R0IC05_9BRAS            Unreviewed;       514 AA.
AC   R0IC05;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CARUB_v10021675mg {ECO:0000313|EMBL:EOA34173.1};
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:EOA34173.1, 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; KB870806; EOA34173.1; -; Genomic_DNA.
DR   RefSeq; XP_006301275.1; XM_006301213.1.
DR   AlphaFoldDB; R0IC05; -.
DR   STRING; 81985.R0IC05; -.
DR   GeneID; 17896448; -.
DR   KEGG; crb:17896448; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   OrthoDB; 1120702at2759; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06098; phytepsin; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   Gene3D; 1.10.225.10; Saposin-like; 1.
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   InterPro; IPR033869; Phytepsin.
DR   InterPro; IPR007856; SapB_1.
DR   InterPro; IPR008138; SapB_2.
DR   InterPro; IPR011001; Saposin-like.
DR   InterPro; IPR008139; SaposinB_dom.
DR   PANTHER; PTHR47966:SF35; ASPARTIC PROTEINASE A2; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   Pfam; PF05184; SapB_1; 1.
DR   Pfam; PF03489; SapB_2; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SMART; SM00741; SapB; 2.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF47862; Saposin; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
DR   PROSITE; PS50015; SAP_B; 2.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..514
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004343483"
FT   DOMAIN          90..511
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DOMAIN          320..360
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   DOMAIN          384..425
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   DISULFID        121..127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   514 AA;  55559 MW;  3EE89578EFB5641E CRC64;
     MVIDSRKVAV SLLVSLLLFV SVSSERNDDG TFRVSLKKLK LDPHNRLAAR FGSNQEKALK
     SSLRSYSNNL GGDSGDTDIV ALKNYLDAQY YGEIAIGTPP QKFTVIFDTG SSNLWVPSGK
     CFFSLSCFFH AKYKSSRSST YKKSGKRAAI HYGSGSISGF FSSDAVTVGD LVVRDQEFIE
     ATSEPGLTFL VAKFDGLLGL GFQEISVGNA TPVWYNMLTQ GLIKKPVFSF WLNRDPKSEE
     GGEIVFGGVD PKHFRGEHTY VPVTQRGYWQ FDMGEVLIAG ESTGYCGSGC SAIADSGTSL
     LAGPTAVIAM INKAIGASGV VSQQCKTVVD QYGQTILELL LAKTQPKKIC SQIGLCTFDG
     TKGVSMGIES VVDKETAKLS NGLRGAGCPA CEMAVVWIQS QLRQNMTQER IVNYVNEMCE
     RMPSPNGESA VDCSQLSKMP TVSFTIGGKV FDLAPEEYIL KIGEGPVAQC ISGFTALDIP
     PPRGPLWILG DVFMGKYHTV FDFGNERVGF AEAV
//
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