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Database: UniProt
Entry: S8D3H2_9LAMI
LinkDB: S8D3H2_9LAMI
Original site: S8D3H2_9LAMI 
ID   S8D3H2_9LAMI            Unreviewed;       755 AA.
AC   S8D3H2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=M569_00464 {ECO:0000313|EMBL:EPS74284.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS74284.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS74284.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
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:EPS74284.1}.
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DR   EMBL; AUSU01000121; EPS74284.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8D3H2; -.
DR   MEROPS; S08.A39; -.
DR   OrthoDB; 11910at2759; -.
DR   Proteomes; UP000015453; 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; 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:UP000015453};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..755
FT                   /note="Subtilisin-like protease"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004549419"
FT   DOMAIN          22..93
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          116..598
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          365..452
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          652..752
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        125
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        538
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EPS74284.1"
FT   NON_TER         755
FT                   /evidence="ECO:0000313|EMBL:EPS74284.1"
SQ   SEQUENCE   755 AA;  79626 MW;  3FEDDAB71106CE09 CRC64;
     FLLCFFFFGL LVVQIHGQHG AYIVWVDASA KPTVFPTHYH WYSSQFAEPA KIIHVYDTVV
     SGFSALLTPS QAALLQENPA VLAALPDRRR QLHTTRSPQF IGLRTQRGLW SESDYGSDVI
     VGVFDTGIWP ERRSFSDLKL GPVPERWRGT CETGVEFSVT NCNRKIIGAR FFSKGHEAAS
     GFGGIIGGIN ETVEFKSARD ADGHGTHTAS TAAGRYAFKA SLEGYASGVA KGVAPKARLA
     VYKVCWKGAG CFDSDILAAF DAAVKDGVDV ISVSIGGGDG VSSPYYLDPI AIGAYAAVSK
     GVFVSSSAGN DGPNGMSVTN LAPWLTTVGA STIDRNFPAD VVLGDGRKFS GASLYAGKPL
     DGKMYPLTYP GKSGVLSSSL CMEDSLDENT VRGKIVICDR GSNPRVAKGL VVKKAGGVGM
     ILANGVSNGE GLVGDAHLIP ACSVGSREGD QIKSYLSSSS SAATATINFR GTVIGVQPAP
     VVASFSSRGP NGLNPQILKP DLIAPGVNIL AAWTDAIGPT GLDSDNRKTE FNILSGTSMA
     CPHVSGAAAL LKSAHPDWSP AAIRSAMMTT ASLVDNSLSP MSDEANQKPA TPYDYGAGHL
     NLDLAMDPGL VYDISGDDYV NFLCAIDYSP KTIQVITGST ARCPKIKKNP EELNYPSISV
     LLSGKEKVSR KSLLRVVTNV GDANSVYRVR VEEPRGVSVS VTPEKLVFSE RVRKLGYYVT
     VSGDGLGDSG AGFGSISWTD GKQHVVRSQI LVVAL
//
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