ID B9S023_RICCO Unreviewed; 500 AA.
AC B9S023;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Aspartic proteinase oryzasin-1, putative {ECO:0000313|EMBL:EEF43206.1};
DE EC=3.4.23.40 {ECO:0000313|EMBL:EEF43206.1};
GN ORFNames=RCOM_1004030 {ECO:0000313|EMBL:EEF43206.1};
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; EQ973835; EEF43206.1; -; Genomic_DNA.
DR RefSeq; XP_015574688.1; XM_015719202.1.
DR AlphaFoldDB; B9S023; -.
DR STRING; 3988.B9S023; -.
DR MEROPS; A01.020; -.
DR GeneID; 8261920; -.
DR eggNOG; KOG1339; Eukaryota.
DR InParanoid; B9S023; -.
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 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; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF20; EUKARYOTIC ASPARTYL PROTEASE FAMILY PROTEIN; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..500
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002891433"
FT DOMAIN 77..497
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 307..347
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DOMAIN 370..411
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT ACT_SITE 95
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 282
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 108..114
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 273..277
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 500 AA; 55147 MW; D9BB7313ED33FB80 CRC64;
MTSIGSMGFR FLLVALCLGA WLGASSSSRL VKIGLKKRRL DLYSINAARI TIADASASFG
WPKADVVYLK NYLDTQYYGE VAIGSPPQTF TVVFDTGSSN LWVPSSKCVL SITCYFHSKF
RAKMSRTYTK IGLPCKIDYG SGSISGFFSQ DYVKLGDATV RDQEFVEVTR EGLLAFLGTQ
FDGILGLGFQ EITVGQATPV WYNMVRQGHV NQKLFSLWLN RDPTAGMGGE IVFGGLDWRH
FRGEHTYVPV TEKGYWQIEV GDVFIAKKST GMCEYGCAAI VDSGTSFIAG PTTIVTQINH
AIGAQGIVSL ECKSVVTKFG DLIWESLISG LRPEIVCVDI GLCVYNNNSR TVIKTKADDR
DGDKSSSLDE SALCTFCEMI VFWIQVQLKQ QKAEEKIFKY VDELCEKLPD PMGKSFIDCG
DITNMPYVTF IIGNKSFPLS PEQYVVKVEE KYGTICLSGF TALDVPPPQG PLWILGDVFL
GAYHTVFDFG NLRIGFARAA
//