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Database: UniProt
Entry: A0A218WGH0_PUNGR
LinkDB: A0A218WGH0_PUNGR
Original site: A0A218WGH0_PUNGR 
ID   A0A218WGH0_PUNGR        Unreviewed;       762 AA.
AC   A0A218WGH0;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Subtilisin-like protease SBT1.7 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CDL15_Pgr017827 {ECO:0000313|EMBL:OWM71944.1};
OS   Punica granatum (Pomegranate).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Punica.
OX   NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM71944.1, ECO:0000313|Proteomes:UP000197138};
RN   [1] {ECO:0000313|Proteomes:UP000197138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX   PubMed=28654223; DOI=10.1111/tpj.13625;
RA   Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA   Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT   "The pomegranate (Punica granatum L.) genome and the genomics of
RT   punicalagin biosynthesis.";
RL   Plant J. 91:1108-1128(2017).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWM71944.1}.
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DR   EMBL; MTKT01004293; OWM71944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218WGH0; -.
DR   Proteomes; UP000197138; Unassembled WGS sequence.
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; 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; IPR023827; Peptidase_S8_Asp-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:SF463; OS12G0427600 PROTEIN; 1.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 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; PS00136; SUBTILASE_ASP; 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..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..762
FT                   /note="Subtilisin-like protease SBT1.7"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012804213"
FT   DOMAIN          48..129
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          152..582
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          381..468
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          663..759
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   REGION          208..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        161
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        223
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        549
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   762 AA;  79865 MW;  1C0CF0094A85FEE3 CRC64;
     MDEKKLSNSP IMVFFLASLI LVLGVPRGLA DSKVSSAILK RDQDAVSTYI VHVEKPMGRL
     FSEEEDLDSW YQSYLPVSLS SSGQQPTIVH SYRNVITGFA ARLTAEQAEA LKSMKGVVYT
     KRERILSLHT THSPAFLGLY QQLSLWKEAN LGKGVIIGVL DSGVDPNHPS FSDEGMPPPP
     VTWKGKCEFR ATECNNKLIG ARNFINSGGK ASAVPPPRDE EGHGTHTSST AAGNFVPGAN
     ALGMASGMAS GMAPLAHLAI YKVCSEEGCG ESDILAAMDA AIADGVDVLS LSLGGGSVPF
     FDDSIAIGAF AAMEKGIFVS CSAGNDGPLN STLSNEAPWI LTVGASSIDR TIKATARLGN
     AGTYDGESLF QPKDFPSRLV PLVYAGANGN SSSALCAEGS LRNSNVRGKV VLCERGGGIA
     RIAKGQEVKD AGGAAMILMN DELNAYSTLV DAHVLPATHV SYAAGLKIKG YINSTSTPTA
     TIAFKGTIIG DPSAPAVTSF SSRGPSIESP GILKPDIIGP GVSILAAWPF PIENDTKTTV
     NFNIISGTSM SCPHLSGVAA LLKSAHPDWS PAAIKSAIMT TANVFNLAKK PIINENLLPA
     DIFTIGAGHV NPAKASDPGL IYDVSPVEYI AYLCGLGYSD KEIAFVTQKN VSCSSVRSIP
     EAQLNYPSFS IILGSSPQNY TRTVTNVGST GSYTYKVDAP DGVDVTVSPS MLKFSGTGQS
     ATYTVAFSRS SSGSTGKPFS QGSVTWVSDR YVVRSPIAVI FK
//
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