ID B9RUD5_RICCO Unreviewed; 742 AA.
AC B9RUD5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Xylem serine proteinase 1, putative {ECO:0000313|EMBL:EEF44922.1};
DE EC=3.4.21.25 {ECO:0000313|EMBL:EEF44922.1};
GN ORFNames=RCOM_0851880 {ECO:0000313|EMBL:EEF44922.1};
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; EQ973817; EEF44922.1; -; Genomic_DNA.
DR AlphaFoldDB; B9RUD5; -.
DR MEROPS; S08.A22; -.
DR InParanoid; B9RUD5; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-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; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF523; SERINE PROTEINASE 1, PUTATIVE-RELATED; 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; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
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}.
FT DOMAIN 4..88
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 119..571
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 351..442
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 640..737
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 526
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 742 AA; 79814 MW; 96BA126BB9E6AC7D CRC64;
MTRSYVVHLG RHSHASEPSA SDISTIAQSH NEILASCISS KEKAKEAIFY SYTRYFNGFA
ATLEDDEVAE LSKHPNVKAV LPNRENKLQT TKSWEYLGLE KNGEVPAYSL WVKAKFDQDL
IIGTLDSGVW PESESFNDHG MGPIPPKWKG YCETNDGVRC NRKLIGARYF NKGYEAAIGR
PLDASYQTAR DYDGHGTHTL STAGGGFVKG ANFLGSSYGT AKGGSPKARV ASYKVCWPGC
HDADILAAME VAISDGVDIL SLSIGGPPAH YYMDSIALGS FHAVENGILV VCAAGNEGPT
PGTVSNLAPW ILTVAASSID RDFPSNIVLG NKEQFKGKSF KTNTLPVGKY YPLVYSVDVK
AANISSTHAR FCHIGALDPM KVRQKIVYCV RDEYSDVEKS EWFAKAGGVG MILAKHGAGS
EVRPEAYFVP TSMVSAEDGL SILSYIRHTK SPKAYISGAT RLGTVTAPIM ADFSCPGPNS
ITSEILKPDI TAPGVYILAA YTQASGSMPL VTDQFHVPFN IISGTSMACP HVSGISGLLK
AVHPDWSPAA IKSAIMTTAR TRSNVRKPIA NASLVAANPF NYGAGHVWPN RAVNPGLVYD
LTVTDYLKFL CSIGYNSSGL LSLFVDVTYE CQSREAGPSD LNYPSITVPS LSGKVTLSRT
LKNVGTPSLY KVRVKPPKGI SVKVEPETLK FNKLHEEKKF KVTLEAKGGS SADHGYVFGG
LTWSDGKLYV VKSPIVVKKA VG
//
