ID A0A059DE83_EUCGR Unreviewed; 770 AA.
AC A0A059DE83;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Subtilisin-like protease SBT5.3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=EUGRSUZ_A01377 {ECO:0000313|EMBL:KCW89053.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW89053.1};
RN [1] {ECO:0000313|EMBL:KCW89053.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW89053.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; KK198753; KCW89053.1; -; Genomic_DNA.
DR RefSeq; XP_010048342.1; XM_010050040.2.
DR AlphaFoldDB; A0A059DE83; -.
DR MEROPS; S08.119; -.
DR EnsemblPlants; KCW89053; KCW89053; EUGRSUZ_A01377.
DR Gramene; KCW89053; KCW89053; EUGRSUZ_A01377.
DR eggNOG; ENOG502QT1T; Eukaryota.
DR InParanoid; A0A059DE83; -.
DR OMA; MELEHNG; -.
DR OrthoDB; 11910at2759; -.
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; 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:SF688; SUBTILISIN-LIKE PROTEASE SBT5.3; 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; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..770
FT /note="Subtilisin-like protease SBT5.3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001575277"
FT DOMAIN 28..113
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 142..618
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 401..475
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 672..767
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 560
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 770 AA; 82154 MW; 6CFDBD2E8E5B6299 CRC64;
MSLSVHLLVL VLLSLTPHQT PAFAAKKSYV VYLGSHSHGR DASLADLSRV TESHHEFLGS
FLGSRDDAEE AIFYSYTRHI NGFAATLEDE VAAQIAKHPR VVSVFLNQGK KLHTTRSWEF
LGLEQNGVIP SESIWKKARF GEDIIIGNLD SGAWPESKSF SDQGLGPIPP KWKGICQNDK
DPRFRCNRKL IGARYFNQGY AAAVEPLSAS FDTPRDNEGH GSHTLSTAGG NFVAGASVFG
YGRGTAKGGS PKARVAAYKV CGPPVAAGAC FDADIMAGFD AAIHDGVDVL SVSLGGSPPL
PTLLNDSIAI GSFHAVTNGI VVVCSAGNDG PGDRTVSNIW PWLITVAAST MDRDFSNYVV
IGDQRRFKGA SLSPKSLPGG KFYKLISAAD AGLSHVSPDE AIFCKDGTLD PRKVKGNILV
CLWGENATVH EGEQAFLAGA VGMVLANSIL SGNEILADPH LLPASHVNYG DGAAIFSYIK
STKFPTAQIT RVVTNLGVKP SPLMAAFSSK GPNTITPEIL KPDITAPGVS VIAAYTEAAG
PTDEEFDKRR VPFNAVSGTS MSCPHVSGVA GLLKTLHPEW SPAAIRSAIM TSATIQDNAM
ESIINASYYK ATPFSYGAGH IQPNRAMDPG LVYDLGIEDY PNFLCSLGYN AMQISMFSDG
AYNCSKHIGL LDFNYPSITV PKLSGSIMVT RTVKNVGLPG TYRASILEPN GVSVLVKPAY
LKFKKINEKK SFKVVLKAKG ASVTGDYSFG ELIWSDTEHY VRSPIVVKAI
//
