ID A0A2I4EWI9_JUGRE Unreviewed; 780 AA.
AC A0A2I4EWI9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Subtilisin-like protease SBT1.6 {ECO:0000313|RefSeq:XP_018823763.1};
GN Name=LOC108993340 {ECO:0000313|RefSeq:XP_018823763.1};
GN ORFNames=F2P56_029462 {ECO:0000313|EMBL:KAF5448972.1};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018823763.1};
RN [1] {ECO:0000313|EMBL:KAF5448972.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5448972.1};
RA Martinez-Garcia P.J., Crepeau M.W., Puiu D., Gonzalez-Ibeas D., Whalen J.,
RA Stevens K., Paul R., Butterfield T., Britton M., Reagan R., Chakraborty S.,
RA Walawage S.L., Vasquez-Gross H.A., Cardeno C., Famula R., Pratt K.,
RA Kuruganti S., Aradhya M.K., Leslie C.A., Dandekar A.M., Salzberg S.L.,
RA Wegrzyn J.L., Langley C.H., Neale D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF5448972.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5448972.1};
RA Marrano A., Britton M., Zimin A.V., Zaini P.A., Workman R., Puiu D.,
RA Bianco L., Allen B.J., Troggio M., Leslie C.A., Timp W., Dendekar A.,
RA Salzberg S.L., Neale D.B.;
RT "Walnut 2.0.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_018823763.1}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018823763.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; LIHL02000013; KAF5448972.1; -; Genomic_DNA.
DR RefSeq; XP_018823763.1; XM_018968218.2.
DR STRING; 51240.A0A2I4EWI9; -.
DR EnsemblPlants; Jr13_08960_p1; cds.Jr13_08960_p1; Jr13_08960.
DR GeneID; 108993340; -.
DR Gramene; Jr13_08960_p1; cds.Jr13_08960_p1; Jr13_08960.
DR KEGG; jre:108993340; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000235220; Chromosome 13.
DR Proteomes; UP000619265; 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; 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; 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:SF810; SUBTILISIN-LIKE PROTEASE SBT1.6; 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; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000235220};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..780
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041062552"
FT DOMAIN 37..108
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 131..604
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 383..468
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 669..774
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 555
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 780 AA; 82707 MW; 69D6080CFF8A3DDB CRC64;
MASDSIPPLL FFISFLFLCS FPPQIPAVST DQSARTFIFR VDSHSKPSIF PTHYHWYASE
FADAPRILHV YDTVFHGFSA TLTPDEANSL GQHPSVLAVF EDRRRQLHTT RSPQFLGLRN
QRGLWSNSDY GSDVIVGIFD TGIWPERRSF SDKNLGPVPV RWKGACEIGE KFVARSCNRK
LIGARFFVKG HEAAGAGSGG VPPITMVNDT VEYRSPRDAD GHGTHTASTA AGRYAFQASM
AGYASGIAKG VAPKARLAVY KVCWKNSGCF DSDILAAFDK AVADGVDVIS ISIGGGDGIS
SPYYLDPIAI GAYGAVSRGV FVSSSAGNDG PNVMSVTNIA PWLMTVGAGT IDRDFPAIVT
LGNMRKLYGV SLYAGAQLNG TMYPLVYPGK SGVFSASLCM ENSLNPNLVR GKIVICDRGN
SPRVAKGLVV KKAGGVGMIL ANGVYNGEGL VGDAHLLPAC AIGADEGELV KKYITSTANP
TATIDFRGTL LGIKPAPVVA SFSGRGPNGL NPEILKPDLI APGVNILAAW TDAVGPTGLD
TDTRKTEFNI LSGTSMAAPH VSGAAALLKS AHHDWSPAAI RSAMMTTASI IDNRNQPMLD
ESSGKPSTPY DFGSGHLNLD RAIDPGLVYD ITNDDYVKFL CSIGYGPKII QVITRSPASC
PVKKPVPENL NYPSMAALFP SSSSVGPSSK TFFRTVTNVG PSNAVYVARV EAPKGVTVTV
KPSKLAFTTA VRKQSFVVTV TADTRNLVLD DSGAVFGSLS WSDGNHVVRS PIVVTQLNLL
//
