ID B9SVA7_RICCO Unreviewed; 514 AA.
AC B9SVA7;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 06-MAR-2013, entry version 25.
DE SubName: Full=Aspartic proteinase, putative;
DE EC=3.4.23.40;
GN ORFNames=RCOM_1303660;
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae;
OC Acalypheae; Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale;
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B.,
RA Gedil M., Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M.,
RA Ravel J., Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
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DR EMBL; EQ974163; EEF32480.1; -; Genomic_DNA.
DR RefSeq; XP_002529926.1; XM_002529880.1.
DR GeneID; 8266253; -.
DR KEGG; rcu:RCOM_1303660; -.
DR KO; K08245; -.
DR ProtClustDB; CLSN2926223; -.
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 Gene3D; 1.10.225.10; -; 2.
DR Gene3D; 2.40.70.10; -; 3.
DR InterPro; IPR001461; Peptidase_A1.
DR InterPro; IPR021109; Peptidase_aspartic.
DR InterPro; IPR001969; Peptidase_aspartic_AS.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB.
DR PANTHER; PTHR13683; PTHR13683; 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; 1.
DR SUPFAM; SSF50630; Pept_Aspartic; 1.
DR SUPFAM; SSF47862; Saposin_like; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS50015; SAP_B; 2.
PE 3: Inferred from homology;
KW Aspartyl protease; Complete proteome; Disulfide bond; Hydrolase;
KW Protease.
SQ SEQUENCE 514 AA; 55834 MW; 6D5ADE1AD6CF6F52 CRC64;
MGTIFKPALF FCLILLPLVC ATASSSNDGL VRIGLKKRKF DQNNRVAAQF ESKEGEAFRA
SIKKYHIRGN LGDAEDIDIV SLKNYMDAQY FGEIGIGTPP QKFTVIFDTG SSNLWVPSSK
CYFSVACYFH SKYKSGQSST YKKNGKSADI HYGTGAISGF FSQDNVKVGE LVIKNQEFIE
ATREPSITFL VAKFDGILGL GFQEISVGNA VPVWYNMVNQ GLVKEPVFSF WFNRNADEDE
GGEIVFGGMD PNHYKGEHTY VPVTQKGYWQ FDMGDVLIDG KTTGICSSGC AAIADSGTSL
LAGPTTIITE VNHAIGATGV VSQECKAVVA QYGETIIAML LAKDQPQKIC SQIGLCTFDG
SRGVSMGIES VVNEKIQEVA GGLHDAMCST CEMAVVWMQN QLKQNQTQEH ILNYVNELCE
RLPSPMGESA VDCGSLSTMP NVSFTIGGRV FDLAPEQYVL KVGDGEAAQC ISGFTALDVP
PPRGPLWILG DVFMGPFHTV FDYGNKRVGF AEVA
//