ID B9SVA7_RICCO Unreviewed; 514 AA.
AC B9SVA7;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE SubName: Full=Aspartic proteinase, putative {ECO:0000313|EMBL:EEF32480.1};
DE EC=3.4.23.40 {ECO:0000313|EMBL:EEF32480.1};
GN ORFNames=RCOM_1303660 {ECO:0000313|EMBL:EEF32480.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
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., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA 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.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; EQ974163; EEF32480.1; -; Genomic_DNA.
DR RefSeq; XP_002529926.1; XM_002529880.2.
DR RefSeq; XP_015581298.1; XM_015725812.1.
DR AlphaFoldDB; B9SVA7; -.
DR SMR; B9SVA7; -.
DR STRING; 3988.B9SVA7; -.
DR GeneID; 8266253; -.
DR KEGG; rcu:8266253; -.
DR eggNOG; KOG1339; Eukaryota.
DR InParanoid; B9SVA7; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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:SF54; ASPARTIC PROTEINASE A1-LIKE; 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 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:UP000008311};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..514
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002891734"
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 ACT_SITE 108
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 295
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 121..127
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
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
//