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Database: UniProt
Entry: B9RBY1_RICCO
LinkDB: B9RBY1_RICCO
Original site: B9RBY1_RICCO 
ID   B9RBY1_RICCO            Unreviewed;       743 AA.
AC   B9RBY1;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Xylem serine proteinase 1, putative {ECO:0000313|EMBL:EEF51052.1};
DE            EC=1.3.1.74 {ECO:0000313|EMBL:EEF51052.1};
GN   ORFNames=RCOM_1682280 {ECO:0000313|EMBL:EEF51052.1};
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 S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; EQ973774; EEF51052.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9RBY1; -.
DR   eggNOG; ENOG502QPQR; Eukaryota.
DR   InParanoid; B9RBY1; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009610; P:response to symbiotic fungus; IEA:UniProt.
DR   CDD; cd02120; PA_subtilisin_like; 1.
DR   CDD; cd04852; Peptidases_S8_3; 1.
DR   Gene3D; 2.60.40.2310; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034197; Peptidases_S8_3.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR045051; SBT.
DR   InterPro; IPR041469; Subtilisin-like_FN3.
DR   PANTHER; PTHR10795:SF557; PEPTIDASE_S8 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Oxidoreductase {ECO:0000313|EMBL:EEF51052.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..743
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002890862"
FT   DOMAIN          40..120
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          143..565
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          366..453
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          645..740
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        152
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        207
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        531
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   743 AA;  78993 MW;  ED9D76530920BB2B CRC64;
     MLLIVLLILA SNFSSSQAVL EKSVYSSTVA NVKEDRNLQT YIVLLEKPEG NQFTESKDLD
     SWYQSFLPDN SFSSNQPRLL HSYRHVVTGF AAKLTADEVQ AMNKKKGFVS ARPRRMVPLH
     TTHTPSFLGL QQNLGFWNYS NYGKGVVIGL IDSGITADHP SFSGEGLPPP PAKWKGKCDN
     GTLCNNKLIG VRNFATDSNN TLDEYMHGTH TASTAAGSPV QNANYFGQAN GTAIGMAPLA
     HLAMYKVSGR FGKAGDSEIL AAMDAAIEDG VDVLSLSLGI GSHPFYDDVI ALGAYAAIQK
     GIFVSCSAGN SGPDSSSLSN EAPWILTVGA SSVDRAIRAT VLLGNNTELN GESLFQPNDS
     PSTLLPLVYA GASGTGSSAY CEPGSLSNFD VKGKIVLCER GGSYETVLKG QEVKDNGGFA
     MIVMNDEFDG FVTEAEFHVL PASHVSYMAG LAIKTYINST STPKATIVFK GTVLGLPEAP
     QVADFSSRGP SVASPGILKP DIIGPGVRIL AAWPVSVDNT TNRFDMISGT SMSCPHLSGI
     GALLRSAHPD WSPAAIKSAI MTTANMVNLG GKLISDQEFV LSTVFDIGAG HVNASGANDP
     GLIYDIQPDD YIPYLCGLGY SDKQVGLIVQ RAVKCSNDSS IPEAQLNYPS FSINLGPTPQ
     TYTRTVTNVG KPDSTYFIEY SAPLGVDIEV TPAELIFSRV NQKATYSVTF SKNGNAGGTF
     VDGYLKWVAN GYNVRSVIAV TFE
//
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