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Database: UniProt
Entry: A0A067KCQ4_JATCU
LinkDB: A0A067KCQ4_JATCU
Original site: A0A067KCQ4_JATCU 
ID   A0A067KCQ4_JATCU        Unreviewed;       765 AA.
AC   A0A067KCQ4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Subtilisin-like protease SBT1.8 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=JCGZ_07493 {ECO:0000313|EMBL:KDP33922.1};
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:KDP33922.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP33922.1, 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:KDP33922.1};
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; KK914539; KDP33922.1; -; Genomic_DNA.
DR   RefSeq; XP_012077058.1; XM_012221668.1.
DR   AlphaFoldDB; A0A067KCQ4; -.
DR   MEROPS; S08.A24; -.
DR   GeneID; 105637972; -.
DR   KEGG; jcu:105637972; -.
DR   OrthoDB; 11910at2759; -.
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   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:SF335; SUBTILISIN-LIKE PROTEASE SBT1.8; 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: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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..765
FT                   /note="Subtilisin-like protease SBT1.8"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001639471"
FT   DOMAIN          27..103
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          133..582
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          375..458
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          661..758
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   REGION          201..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        141
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        216
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;  81361 MW;  164493E56760A1D0 CRC64;
     MGNMACISFL SILLLLAFSF SVTAKQTYIV HMKHNAKPES FATHHDWYSA SLQSITSASD
     SLLYTYTTAF PGFAASLDPE EVDSLRNSDA VLDVYEDTIY SLHTTRTPQF LGLSTDLGFF
     NGHTTLDIDQ ASHDVVIGVL DTGVTPGSKS FDDSGMPEIP TRWKGECESA QDFSPTLCNK
     KLIGARYFSK GYRMASGGGY LRKPKEIESP RDQDGHGTHT ASTAAGSQVA NASLLGYASG
     TARGMAPHSR VAAYKVCWNT GCFGSDILAG MDRAIADGVD VLSLSLGGGS APYYRDTVAI
     GAYSAMERGI FVSCSAGNSG PNRATLANVA PWIMTVGAGT LDRDFPAYAV LGDKSRFSGV
     SLYSGTGMGN KLVGLVYNKR NISSNLCLPG SLEPTMVRGK VVVCDRGINA RVEKGAVVRD
     AGGIGMILAN TAASGEELVA DSHLLPAVAV GRKAGDKIRE YVSNHPNPTA LLSFGGTVLN
     VRPSPVVAAF SSRGPNMVTP QILKPDLIGP GVNILAAWSD SVGPTGLEKD TRKTQFNIMS
     GTSMSCPHIS GVAALLKAAH PSWSPSAIKS ALMTTAYVVD NTNSPLRDAG SDVAGAFSNP
     WAHGSGHVDP HKALTPGLVY DISTQEYEAF LCSLGYTIDH VQAIVKRPNV TCSKKFRDPG
     ELNYPSFSVV FASKRVVRYT RELTNVGEAG SIYEVAVNGP STVGVTVKPT KLVFKNVGDK
     LRYTVTFVAK KGANQDARSE FGSIVWRNAQ HQVRSPIAFT WTHLL
//
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