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Database: UniProt
Entry: A0A067KWL2_JATCU
LinkDB: A0A067KWL2_JATCU
Original site: A0A067KWL2_JATCU 
ID   A0A067KWL2_JATCU        Unreviewed;       765 AA.
AC   A0A067KWL2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDP40601.1};
GN   ORFNames=JCGZ_24600 {ECO:0000313|EMBL:KDP40601.1};
OS   Jatropha curcas (Barbados nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC   Jatropha.
OX   NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP40601.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP40601.1, ECO:0000313|Proteomes:UP000027138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:KDP40601.1};
RX   PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA   Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT   "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT   L.) Seedlings Exposed to Salt Stress.";
RL   PLoS ONE 9:E97878-E97878(2014).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; KK914327; KDP40601.1; -; Genomic_DNA.
DR   RefSeq; XP_012068759.1; XM_012213369.1.
DR   AlphaFoldDB; A0A067KWL2; -.
DR   MEROPS; S08.104; -.
DR   GeneID; 105631293; -.
DR   KEGG; jcu:105631293; -.
DR   OrthoDB; 662485at2759; -.
DR   Proteomes; UP000027138; 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   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; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
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:SF549; OS01G0278950 PROTEIN; 1.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 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:UP000027138};
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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..765
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001639907"
FT   DOMAIN          30..114
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          143..600
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          660..756
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        151
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        210
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        543
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   765 AA;  82771 MW;  15AEC37DBA2194C8 CRC64;
     MASLLLLLLL SFLPFPIISS TISIQTTKPY IVYMGSSWNF DHNARIDATI AESAHLQILS
     SIIPSQESER ISLIHSYHHA FRGFCAMLTE DEASLLSDHV EVLSVFPDPK LQLHTTRSWD
     FLYSLSGIGS KLGHQHHHHH LSNDVIIGVI DTGIWPESPS FKDDHIGQIP SRWKGVCEEG
     SDFNKSNCNR KLIGARYYIS GGSPRDALGH GTHCASIAAG APVANASFYG LARGTARGGA
     PAARIASYNV CKGRNCSGST VLKAIDDAIK DGVDIISVSL GLTSPTQPKF LEDPVAIGAF
     HAEERGVMVI SSAGNQGPDA FTVSNTAPWI LSVAASSIDR DFQSTVVLGN GRTIKGSAIN
     FSNLSRSKMY PLVLGEDVAI NNTLVSDARQ CIPGSLDPEK ASGKIIVCIT SDPTIRTELA
     EAKGLILVAE ILEVPHTSTG SFPFTEVRKN AEHMILNYIK STKKPKATIL PSVDVLGVRP
     SPVVAYFSSR GPGNLTENIL KPDIMAPGQE ILAAVIPTDN EVDGPDILNG KKPLKFGIKS
     GTSQACPHVS GAAALIKSVH PTWSSSIIRS ALMTTAIIFN NNGKPLTNDS DYRANPHEMG
     VGEISPVRAL DPGLVFETEV KDYLHFLCYY GYPKEKVRAM SKTKINCPEN SNEELISSSI
     NYPSISIGKL DQNKPAHTIT RRVTNLGPAN SSYYSTVYAP KGLQVKVYPE KLTFDEGKRR
     ASFRVLFNGK KASKGYNFGN VIWSDGHHRV RVVFAVNVVS PNTLF
//
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