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
//