ID S8CZR8_9LAMI Unreviewed; 810 AA.
AC S8CZR8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 08-NOV-2023, entry version 40.
DE RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=M569_01766 {ECO:0000313|EMBL:EPS72989.1};
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:EPS72989.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS72989.1, 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:EPS72989.1}.
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DR EMBL; AUSU01000610; EPS72989.1; -; Genomic_DNA.
DR AlphaFoldDB; S8CZR8; -.
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; 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:SF384; SUBTILISIN-LIKE PROTEASE SBT2.6; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 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 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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..810
FT /note="Subtilisin-like protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004562339"
FT DOMAIN 17..121
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 148..629
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 713..806
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 231
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 592
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:EPS72989.1"
FT NON_TER 810
FT /evidence="ECO:0000313|EMBL:EPS72989.1"
SQ SEQUENCE 810 AA; 86831 MW; E34484CACCFA0C6C CRC64;
IVLILISFLI FGKSEIYIVT LEGEPVVSYR GGVDGFEATA ADLDLDEELD VTSESAVLYA
RHLERRHDLL LDMLFEQGSF KKLYSYRHVI NGFAVHLTPE QADILVQAPG VKSVDRDWKV
RRLTTHTPEF LGLPTGVWPT GGGFDRAGED IVIGFVDSGI YPHHLSFATN NAEHYGPVSR
FRGKCEVDRH TNRDFCNGKI VGAQHFAEAA KAAGAFNPDV DFDSPLDGDG HGSHTAAIAA
GNNGIPVRMH GFEFGRASGM APRARIAVYK ALYRLFGGFV ADVVAAIDQA VHDGVDILNL
SLGPNSPPAT TKTTFLNPFD ATLLSAVKAG VFVVQAAGNG GPFPKSLVSY SPWITTVAAA
VDDRRYKNHL TLGNGKILAG IGLSPSTHGN RSYTLVAAND VLLDSAAKYG PFDCQRPEVL
NKNLVQGKIL LCGYSFNFVS GTSSVKIVAQ TARTLGAAGF VLAVENAYPG TKFDPVPVAV
PGIVITDSDK SMELINYYNT STPRDWTGCV KSFDAVGYIG DGLRPILHKS APIVALFSAR
GPNIKDYSFQ DADLLKPDIL APGSLIWAAW SLNGTDEPNY LGEGFAMISG TSMAAPHIAG
IAALVKQKYP HWSPAAIKSA LMTTSTTVDR AELPLRALQY APGSENLSLV QATPFDYGSG
HVNPRAALDP GLVFDSGYED YLGFLCTTRG IDTNEVRNYT HVPCNYTLGH PSNLNVPSVT
ISRLVGSQTV TRTVTNVAEE EETYTIQARM GPAVAIEASP AAMTLLPGAS GKFTVTLTPR
TITGTYSFGE IWLKGSRGHK VRIPVVAMGY
//
